The basis of the atomic theory. Stoichiometry. Types of chemical reactions and solution stoichiometry. Properties of gases. Chemical equilibrium. Acids and bases. Applications of aqueous equilibria. Chemical thermodynamics. Enthropy, free energy and equilibrium. Electrochemistry. Chemical kinetics. Physical properties of solutions.

Molar volume of gases, thermochemistry, reaction enthalpies and Hesse's law, Rate of chemical reactions, decomposition of hydrogen peroxide, reaction reversibility and Le Chatelier's principle, determination of acid ionization constants, oxidation-reduction; electrochemistry, thermodynamics of an electrochemical cell.

Lectures:
I. Introduction: The study of life; major themes and approaches.

II. The evolution of life: Basis of ideas on evolution and the tree of life. Classification of organisms, major groups,their characteristics and evolutionary history, covering viruses, prokaryotes and eukaryotes, protists, fungi, algae, plants, invertebrates and vertebrates.

III. Structure and function of plants and animals: Plants; structure and growth, vascular systems, photosynthesis, nutrients and reproduction. Animals (emphasis on vertebrates); structure and major tissues of the body, nutrition and digestion, signalling systems of hormones, vascular systems and respiration, excretory- and reproductive systems, development, nervous system and movements, sensory systems.

IV. Ecology: The major biomes of the earth and the distribution of organisms, behavioural ecology, population ecology, structure and dynamics of communities and ecosystems, diverse ecosystems, conservation and global ecology.

Practicals: The course involves four practical exercises.
Evaluation: A written final exam 80%, practical reports 20%. Students need to pass both components (minimum grade 50/100).

Undergraduate biology students are not allowed to take this course

Lectures: Mendelian inheritance. Sex chromosomes. Cytoplasmic inheritance. Chromosomes. Cell division (mitosis and meiosis). Life cycles. Linkage and recombination in eukaryotes. Bacterial genetics. Gene mapping and tetrad analysis. Genotype and phenotype. Chromosomal changes. DNA: Structure and replication. RNA: Transcription. Rgulation of gene transcription. Gene isolation and manipulation. Genomics. Transposons.  Mutations. Repair and recombination.  Model organisms. Laboratory work: : I. The fruitfly Drosophila melanogaster. II. Mitosis in onions. III. Plasmids and restriction enzymes. IV. PCR. V. Analysis of asci from Sordaria fimicola.

Exam: Laboratory and problems 25%, written 75%. Minimum mark needed for each part.

Course description: The fundamental concepts of calculus will be discussed. Subjects: Limits and continuous functions. Differentiable functions, rules for derivatives, derivatives of higher order, antiderivatives. Applications of differential calculus: Extremal value problems, linear approximation. The main functions in calculus: logarithms, exponential functions and trigonometric functions. The mean value theorem. Integration: The definite integral and rules of integration. The fundamental theorem of calculus. Techniques of integration, improper integrals. Series and sequences. Ordinary differential equations. Vectors and matrix calculations.

This course focuses on the structure of the periodic table and properties of the elements based on their place in the periodic table. The students learn about the naturally occurring forms of the elements, isolation of the elements and common chemical reactions. Atomic theory is taught as a base for understanding the properties of the elements and their reactivity. Early theories of the structure of the hydrogen atome put forward by Bohr and their development to modern view of the atom structure are covered. The electronic structure of the atom is described, and theories describing formation of chemical bonds such as valence bond theory, VSEPR, and molecular orbital theory are used to determine structures and predict reactivity of molecules. Processes for purification of metals from their naturally occurring ores is covered as well as properties of metalloids and nonmetals. The transition metal elements, and the formation of coordination compounds with solubility, equilibria, ions and electron pair donors will be introduced. Radioactivity, formation and types of radioactive species, reactions and their applications will be introduced.

Standardization of a pipette. Quantitative determinations of Ni in steel, Ca in milk, Na in water and wine.  Quantitative analysis of acetic acid and hydrogenperoxide. Identification of amino acid. Quantitative analysis of fluoride using electochemical cells.  Two component analysis using photometry.

During this course, students will be introduced to organisms and acellular entities too small to be seen by the unaided eye.  They can acquire knowledge on the characteristics of bacteria, archaea, viruses and eukaryotic microorganisms.  The course will explain the importance of microorganisms, how they live in diverse and dynamic ecosystems and how some affect humans, for example by being valuable for the food industry or by causing disease.  The students will gain laboratory experience and practice aseptic techniques. 

Evolutionary biology: Darwin and evolution of the evolutionary theory. The tree of life, natural selection and adaptation.  How evolution works: The origin of variation, the raw material for evolution.  The genetical theory of natural selection. Evolution of phenotypic traits.  Genetic drift: Evolution at random and in space. Species and speciation. Products of evolution:  Conflict and cooperation. Life-history evolution. Coevolution among species. Evolution of genes and genomes. Evolution and development. Macroevolution and the history of life: Phylogeny, the history of life, geography of evolution and the evolution of biological diversity. Evolution above the species level. Human evolution and human society.

At the beginning of the course some main statistical concepts are introduced, such as population, sample, variable and randomness. Various descriptive statistics are introduced, as well as basic graphical representations. Fundamentals of probability theory are introduced, as well as the most common probability distributions. The rest of the course deals with inferential statistics where hypotheses tests and confidence intervals for means, variance and proportions are covered as well a analysis of variance (ANOVA) and simple linear regression. Students will learn how to apply the above mentioned methods in the statistical software R.

Organic chemistry appears all around us, both in the biological aspects of our world and in the production aspect of many of our daily products. Organic chemistry also appears in many other subjects, such as biochemistry, pharmaceutical science, food science, and medicine. Understanding of the organic chemistry can help deepen our understanding of  production processes in the chemical and food industry, biochemical pathways, and the manufacturing and bioactivity of drugs.

In this course, we will cover the basics of organic chemistry. We will cover the various functional groups, their properties and reactivity, with a special emphasis on alkanes, alkenes, alkynes, alkyl halides, and aromatic compounds. We will also cover stereochemistry of organic compounds and their analysis and identification using NMR, IR, and MS.

Many of the compounds we use in our daily lives (plastics, medicine, glue and more) are produced via organic chemistry. The pharmaceutical industry is a good example of where it is important to be able to synthesize the right products, isolate/purify them and identify whether the correct product was synthesized. In this course, students will be trained in the main laboratory techniques of organic chemistry and can be beneficial in the chemical industry. Students will also receive training in analyzing their results and writing scientific reports.

Content of course: Energy and the first law of thermodynamics. Chemical thermodynamics. Entropy and the second law of thermodynamics. The third  law of thermodynamics. Free energy. Phase equilibrium. Solutions, in particular ionic solutions. Chemical equilibrium. Electrochemistry. Transport processes: gas kinetics, diffusion and heat transport. Mechanism and rate of chemical reactions. Enzyme catalysis.

Text book:  Atkins' Physical Chemistry 11th Edition

A thorough treatment of the fundamentals of biochemistry - part one; structure and function of macromolecules. The scope of biochemistry. Water and its properties. Interactions in biomolecules. Amino acids, peptides and the structure of proteins. Protein function.  Protein stability, folding, and dynamics related to function. Carbohydrates and glycobiology. Lipids, membranes and membrane proteins. Enzyme kinetics, regulation of enzyme activity, and mechanisms of enzyme catalysis. Signal transduction and membrane receptors. Structure of nucleic acids, stability, and basic recombinant technology. Final grade is combined from the final exam (85% ) and a midterm exam (15%).

Lectures:
Twice weekly (2 x 40 min.) Probelm solving class (2 x 40 min.) weekly.

Course evaluation:
Final exam (3 hours): 85% of final grade.
Midterm: 15% of final grade.

Textbook:
Nelson D.L. & Cox M.M. Lehninger: Principles of Biochemistry, 8th Edition, 2021

The cell biology part includes four lectures each week for 14 weeks (4L week for 14 weeks). The content includes: Introduction to cell biology, structure and evolution of eukaryotic cells. The main emphasis is on eukaryotic cells. Chemistry of the cell and energy conversion, structure and function of cellular macromolecules. The structure and function of cellular organs and functional units like the cell membrane, nucleus, mitochondria, chloroplasts, cytoskeleton, golgi-system, lysosomes and peroxisomes. Intracellular regulation and signal pathways linked to communication between cells, together with cell differentiation and cancer. Details on extracellular matrix are included and basic immunology.

Histology is an independent short course accompanying the LÍF315G cell biology course. The course is structured as a practical course with support lectures, and lectures and practical exercises last for 6 weeks. The practical classes are primarily based on examining histological samples under a microscope and generating properly annotated histological sketches. Attendance is mandatory in practical lessons. The final exam is held two weeks after the last lecture.

The aim of the course is to introduce the basics of histology and tissue structure, as well as to make students independent in the use of microscopes when examining tissue samples. The lectures discuss the properties of individual tissues, the characteristics and function of different cell types and the properties of the extracellular matrix in a tissue-specific context. The preparation of samples is also discussed separately.

Content of course: Principles of quantum mechanics. Chemical bonds. Intermolecular- interactions. Relationship between quantum chemistry and spectroscopy. Spectroscopic methods. Spectral analysis. Introduction to laboratory exercises.

Experiments: Solution calorimeter. Enthalpy of combustion (bomb calorimeter). Phase diagrams and distillation of liquid solutions. Chemical equilibrium and solubility derived from conductivity measurements. Reaction kinetics (rate equations). Electrolyte solutions. Heat of vaporization. Viscosity. Spectroscopy of organic dyes. Chemical equilibrium by spectroscopic methods. Fluorescence of micellar solution. NMR spectroscopy.

Alcohols and phenols, ethers and epoxides, aldehydes and ketones, carboxylic acids, derivatives carbanions, amines, carbohydrates, amino acids and proteins. Spectroscopical identification of organic compounds.

Laboratory work: Synthesis and analytical organic chemistry.

The course is a practical course with weekly supportive lectures.  The lectures provide heroretical background of the instrumental methods and the instruments. The supportive lectures are part of lab exercises and attendance is compulsory.

The students learn about modern methods and instruments used in analytical chemistry based on interaction between chemical- and physical properties of the substances and the electromagnetic field. Chromatographic methods used to separate mixtures into single pure compounds will be introduced.  The focus of the course is the analysis of organic compounds.

Laboratory work: Fluorimetry, atomic absorption, spectrophotometry and applications of IR, UV and visible and NMR spectroscopy. Gas- and liquid (HPLC) chromatography. Gas chromatography/mass spectrometry (GC/MS).

In this course, the main metabolic processes of cells are studied, with a focus on carbohydrate, fat, and protein metabolism, as well as the metabolic regulation of these processes. The course begins with a detailed examination of carbohydrate metabolism, including glycolysis (both aerobic and anaerobic), the citric acid cycle, and the pentose phosphate pathway. Then we continue into pathways such as gluconeogenesis, glycogen breakdown, and then into how carbohydrate metabolism is regulated.

Next, the focus shifts to fat metabolism, where the breakdown of triglycerides, fatty acid oxidation, and fatty acid synthesis are explained. Special emphasis is placed on the regulation of fat metabolism and the control of enzymes involved in these processes. Following this, protein metabolism is addressed, where protein hydrolysis, amino acid degradation, and the urea cycle are studied.

The course also covers the integration and regulation of metabolic pathways, with a focus on the complex regulation that occurs in the key steps of these pathways, considering both intracellular signals and hormones. It examines how these processes adapt to various conditions to maintain homeostasis and the effects of disruptions in their regulation. Lastly, photosynthesis and the Calvin cycle are covered.

This course is highly beneficial for those seeking an in-depth understanding of biochemical processes and the biochemistry of the human body.

Lectures are held twice a week (2 x 40 minutes) over 13-14 weeks. 

This course combines weekly laboratory sessions (6 hours per week for 12–13 weeks) with weekly lectures (2×40 minutes per week for 13–14 weeks).

Lectures provide the theoretical background for the laboratory work and introduce practical applications of the concepts covered.

In the laboratory, students will gain hands-on experience with core techniquesand safety precautions in biochemical research, including:

• Methods for protein purification.
• Quantitative analysis of proteins and specific chemical groups.
• Assessment of protein stability and the effects of ligands.
• Measurement of enzyme kinetics and the effects of inhibitors.
• Use of biochemical databases and related software for research and data interpretation.
• Processing numerical data and the use of linear and nonlinear models on experimental data.
• Proper use of a laboratory notebook and accurate recording of experimental data.
• Writing scientific reports based on experimental findings.

This course provides an introduction to the principles and applications of applied biotechnology, with an emphasis on its role in industry and society. Biotechnology is inherently interdisciplinary, combining elements of molecular biology, chemistry, engineering, and pharmaceutical sciences. Through lectures, group projects, student presentations, and guest seminars, students will explore how biotechnology products and processes are developed — from laboratory research to industrial implementation.

The course is organized around five major areas of applied biotechnology: (1) pharmaceutical biotechnology, (2) Industrial biotechnology in the chemical and food sectors, (3) Clinical biotechnology, (4) Natural product discovery and purification and (5) energy and environmental biotechnology.

This course is based on lectures, project work, student presentations and discussions. One field trip to a biotech company will be done.

The course is co-taught with ILT102F - Introduction to Applied Biotechnology. It is not possible to take both courses.

The course is divided into lectures, practical sessions, discussions and student projects.

Lectures: Theoretical basis of common molecular-biology techniques and their application in research. Course material provided by teachers.

Laboratory practice in molecular biology techniques: Training in general molecular biology laboratory skills and active documentation in laboratory notebooks.

Discussions are associated with all other parts (lectures, practicals and student projects)

Main topics:  Laboratory notebooks, electronic laboratory notebooks and standard operating procedures (SOP's), use of online tools. Basics of DNA work and DNA cloning. Plasmids and plasmid maps, working with DNA sequences. DNA and RNA isolation and quantification (Southern and Northern blotting, PCR, RT-PCR, qRT-PCR), restriction enzymes, DNA sequencing techniques and data analysis. Basics of E. coli cultures and plasmid work. Basics of cell culture and transfection. Model organisms: E.coli, S. cerevisiae, C. reinhardtii, A. thaliana, C. elegans, D. melanogaster, M. musculus.  Transgenesis and genetic tools in bacteria, yeast and multicellular organisms. CRISPR technique and gRNA design. RNA interference and other methods for conditional gene expression and inhibition. Protein expression and analysis. How to raise and use antibodies for research. Western blot, immunostaining of cells and tissues, radioactive techniques. Microscopy in molecular biology. Methods used in recent research papers will be discussed.

Student projects: Study of a recent method or method group. Output varies by year but aims at training students in reference work and different approaches to mediating scientific material. Examples include: Posters, Essays, Talks, Videos, Webpages and Podcasts.

The main purpose of this course is to teach the principles of chemical structure and bonding. The main focus will be on using symmetry and group theory in constructing molecular orbitals for simple molecules and ions. VSEPR and VB methods will also be used to study bonding and structure of molecules. The crystalline solid state, formulas, structures and properties. Each students performance in two interm exams will count as 20% of the final grade. The assignments will count as 5% of the final grade

Generation of carbanions and their reactions, such as alkylation of enolates, C vs. O alkylation, aldol condensation and acylation of carbons. Decarboxylation and formation of double bonds will also be covered, along with organometallic chemistry. General and specific laboratory techniques of synthesis and analysis and the use of databases (Scifinder). Spectroscopic identification of all compounds. 75% of homework must be turned in in order to be allowed to take the exam.

The students will be trained to work independently in the laboratory, which serves as preparation for research projects in graduate school or on the job. Instead of standard and well-tested protocols, like found in most undergraduate laboratory classes, general descriptions from books or journal articles will be used. Each student gets his own four-step synthesis project. The students will carry out the reactions, monitor their progress and isolate the products while documenting their work in their notebooks. They will solve problems that may come up while performing their experiments, including optimization of reaction conditions if the reactions don´t work as expected the first time around. The structures of the products will be verified by spectroscopic methods, in particular NMR.

The students will be shown how to find reaction conditions in journal articles using databases (Scifinder). The lectures will also cover how results are communicated in scientific journals. The students will write an article describing their synthetic work, instead of writing reports for each step. A template from Organic Letters will be used.

The synthesis projects are based on the material covered in EFN511G, where the theme is formation of C-C bonds, for example by alkylation of 1,3-dicarbonyl compounds, by the use of the Wittig and Grignard reactions, aldol condensations etc.

Third year students can elect to work on a specialized 15 ECTS laboratory project under the auspices of a member of the teaching staff depending on availability. The main advisor and the location of the project can be outside the faculty of sciences. If so, a member of staff is responsible for all practical matters. The aim is for the student to gain experience in carrying out research from an initial idea and to a final written report. This will generally give the student the opportunity to gain some new technical skills.
The research project concludes with a report which is graded by the supervisor with consensus from another member of staff. Reports must conform to the format and rules of the Faculty of Physical Sciences.

Lectures: Mendelian genetics, organization of the human genome, structure of chromosomes, chromosomal changes and syndromes, gene mapping via association and whole genome sequencing methods, genetic analysis, genetic screening, genetics of simple and complex traits, genes and environment, cancer genetics, gene therapy, human and primate evolution, ethical issues concerning human genetics, informed consent and private information. Students are expected to have prior knowledge of the principles genetics.

Practical: Analyses of genetic data, study of chromosomal labelling, analyses of genetic associations and transcriptomes.

Note: Only one course of either TÖL101G Tölvunarfræði 1 or TÖL105G Tölvunarfræði 1a can count towards the BS degree.

The Java programming language is used to introduce basic concepts in computer programming: Expressions and statements, textual and numeric data types, conditions and loops, arrays, methods, classes and objects, input and output. Programming and debugging skills are practiced in quizzes and projects throughout the semester.

The immune system, organs and cells. Innate immunity, phagocytes, complement, inflammation. Adaptive immunity, development and differentiation of lymphocytes. Specificity and antigen recognition, function of B- and T-cells. Immune responses, immunological memory, mucosal immunity. Immunological tolerance and immune regulation. Immune deficiency, hypersensitivity, autoimmunity and transplantation.  Treatment and intervention of autoimmune and allergic diseases.  Vaccination and protection from infections. Immunological methods and diagnostics. Students presentations and discussions of scientific articles under the teachers supervision.

Subject Matter: Newtonian Mechanics for particles and rigid bodies. Dynamical variables and conservation laws. Elements of Fluid Mechanics. Thermodynamics. Elements of Electromagnetism. Laboratory exercises in which students are trained in handling physical instruments, performing measurements and interpreting the data.

The course is thaught in English or Icelandic according to the needs of the students.

The aim of this course is to introduce different applications of microorganisms and to help students develop independent research skills. In the first part of the course, students will visit a geothermal area and subsequently work on a research project where they isolate, identify and study bacterial strains.

The second part will introduce different fields of microbial biotechnology and how they have been shaped by recent progress in microbiology, molecular biology and biochemistry. State of the art will be covered regarding subjects such as microbial diversity as a resource of enzymes and biocompounds; bioprospecting, thermophiles, marine microbes and microalgae, biorefineries (emphasis on seaweed and lignocellulose), enzymes (emphasis on carbohydrate active enzymes), metabolic engineering (genetic engineering, omics), energy-biotechnology, cultivation and fermentation technology. The course will exemplify Icelandic biotechnology where applicable. Cultivation/production technology and yeast will be presented specifically in practical sessions in the brewing of beer.

The third part will cover environmental sampling, microbial communities and biofilms, microbes in aquatic and terrestrial environments, indoor air quality and the impact of molds. Also, water- and food-borne pathogens, risk assessment and surveillance, water treatment, microbial remediation, methane production and global warming. Students will visit waste management and water treatment plants and review and present selected research articles.

Additional teaching one Saturday in end of September or beginning of October.

Programming in Python (for computations in engineering and science): Main commands and statements (computations, control statements, in- and output), definition and execution of functions, datatypes (numbers, matrices, strings, logical values, records), operations and built-in functions, array and matrix computation, file processing, statistics, graphics. Object-oriented programming: classes, objects, constructors and methods. Concepts associated with design and construction of program systems: Programming environment and practices, design and documentation of function and subroutine libraries, debugging and testing of programmes.

The characteristics of protein structures at the different structural levels. How structure determines the different properties of proteins. Structural classes of proteins and their characteristics. Relationship between molecular structure and biological function. Interactions that determine structural stability of proteins. Protein folding and unfolding. Effects of different parameters, e.g. temperature, pH, salts and denaturants on protein stability. Techniques used for determination structure and different properties proteins. Selected topics in protein structure function relationships.

Course plan: Lectures twice per week (2x40 min. each time). Computer lab once per week (2x40 min.). Lab sessions involve training using the WWW to study proteins. Tutorials and practice of using SwissPDBviewer program for solving specific assignments related to topics covered in lectures.

This course focuses on methodology and recent innovations in biochemistry, emphasizing both analytical and computational techniques. It is divided into several modules, each taught by experts in their respective fields. While lectures form the core of the material, additional resources such as articles or book chapters may be assigned when appropriate. Practical demonstrations of research equipment may also be included. Students are expected to submit several assignments throughout the semester.

The course will explore recent research in various specialized areas of biochemistry, and the content of the modules is regularly updated.

Topics covered may include single-molecule spectroscopy, protein mass spectrometry, structural biochemistry, binding affinity and thermodynamics and computational biochemistry.

Lectures: Homeostasis, membrane potentials, neurons, nervous systems, endocrinology, sensory physiology, muscles, circulation, respiration, osmoregulation and excretion, digestion, metabolism, energy balance, reproduction.

Lab work: 1) Membrane potentials and ligands. 2) Somatic nerves/skeletal muscle. 3) Ergometry.
Other assignments: Online exams and review questions, information will be given at the beginning of the course.

Developmental biology unifies multiple subject areas within life- and medical sciences and many fundamental discoveries on molecular and cellular processes come from developmental biology research. The aim of the course is for students to gain broad overview of the main topics of developmental biology and to acquire knowledge of the fundamental aspects of the development of different groups of vertebrates and invertebrates at multiple levels, ranging from the whole organism to the role of molecules in regulating developmental processes.

Main lecture topics: The role of development. Historical overview. Development of unicellular organisms. Reproduction and genetic recombination. Developmental patterns among multicellular animals. Specification and determination of embryonic cell fates. Modern techniques in developmental biology. Controlling gene expression, - developmental genes. Importance of cell interactions. Structure of gametes, fertilization and activation of the egg. Early stages of development in selected invertebrates. Specification of embryonic axes and organs of the fruit fly, -a hierarchical system of gene control. Early stages of development and specification of embryonic axes in amphibias, birds and mammals. Fate of embryonic layers and organogensis in vertebrates. Limb formation in tetrapods. Sex determination, sexual development and development of gametes among invertebrates and vertebrates. Plant development.

In the practical exercises, the aim of the course is for students to gain training and skills in the handling and microscopic analysis of embryos, while also strengthening their knowledge of the main developmental events in different animal groups. Emphasis is also placed on students gaining practice in the use of databases in developmental genetics and genetics.

Practicals: The use of databases and genome browsers; Drosophila embryonic development and metamorphosis; zebrafish development; chick development.

Student presentations: Sudents are required to give two short presentations on course-related topics. The grade for each presentation represents 10% of the total grade for the course. Minimum grade required is 5,0 for both presentations.

Third year students can elect to work on a specialized 15 ECTS laboratory project under the auspices of a member of the teaching staff depending on availability. The main advisor and the location of the project can be outside the faculty of sciences. If so, a member of staff is responsible for all practical matters. The aim is for the student to gain experience in carrying out research from an initial idea and to a final written report. This will generally give the student the opportunity to gain some new technical skills.
The research project concludes with a report which is graded by the supervisor with consensus from another member of staff. Reports must conform to the format and rules of the Faculty of Physical Sciences.

The emphasis is on research articles. Resent research in various field with links to cell biology are included but can vary between years. For each lecture max three research articles are included.

Each student gives a seminar on one research article with details on methods and results. The students write a report (essay) on the article and discusses the results in a critical way.

Examples of topics included in the course: innate immunity, prions, the proteins pontin and reptin, polarized epithelium, development of trachea, data analyses and gene expression, autophagy, the origin of the nucleus.

Lectures: The molecular basis of life (chemical bonds, biological molecules, structure of DNA, RNA and proteins). Genomes and the flow of biological information. Chromosome structure and function, chromatin and nucleosomes. The cell cycle, DNA replication. Chromosome segregaition, Transcription. Regulation of transcription. RNA processing. Translation. Regulation of translation. Regulatory RNAs. Protein modification and targeting. DNA damage, checkpoints and DNA repair mechanisms. Repair of DNA double-strand breaks and homologous recombination. Mobile DNA elements. Tools and techniques in molecular Biology, including Model organisms.

Seminar: Students present and discuss selected research papers and hand in a short essay.

Laboratory work: Work on molecular genetics project relevant to current research. Basic methods such as gene cloning, gene transfer and expression, PCR, sequencing, DNA isolation and restriction analysis, electrophoresis of DNA and proteins will be used.

Exam: Laboratory 10%, seminar 15%, written final exam 75%.

The immune system, organs and cells. Innate immunity, phagocytes, complement, inflammation. Adaptive immunity, development and differentiation of lymphocytes. Specificity and antigen recognition, function of B- and T-cells. Immune responses, immunological memory, mucosal immunity. Immunological tolerance and immune regulation. Immune deficiency, hypersensitivity, autoimmunity and transplantation.  Treatment and intervention of autoimmune and allergic diseases.  Vaccination and protection from infections. Immunological methods and diagnostics. Students presentations and discussions of scientific articles under the teachers supervision.

Medicine, biology, biochemistry, food- and nutrition, and related fields.

The basis of the atomic theory. Stoichiometry. Types of chemical reactions and solution stoichiometry. Properties of gases. Chemical equilibrium. Acids and bases. Applications of aqueous equilibria. Chemical thermodynamics. Enthropy, free energy and equilibrium. Electrochemistry. Chemical kinetics. Physical properties of solutions.

Molar volume of gases, thermochemistry, reaction enthalpies and Hesse's law, Rate of chemical reactions, decomposition of hydrogen peroxide, reaction reversibility and Le Chatelier's principle, determination of acid ionization constants, oxidation-reduction; electrochemistry, thermodynamics of an electrochemical cell.

Lectures:
I. Introduction: The study of life; major themes and approaches.

II. The evolution of life: Basis of ideas on evolution and the tree of life. Classification of organisms, major groups,their characteristics and evolutionary history, covering viruses, prokaryotes and eukaryotes, protists, fungi, algae, plants, invertebrates and vertebrates.

III. Structure and function of plants and animals: Plants; structure and growth, vascular systems, photosynthesis, nutrients and reproduction. Animals (emphasis on vertebrates); structure and major tissues of the body, nutrition and digestion, signalling systems of hormones, vascular systems and respiration, excretory- and reproductive systems, development, nervous system and movements, sensory systems.

IV. Ecology: The major biomes of the earth and the distribution of organisms, behavioural ecology, population ecology, structure and dynamics of communities and ecosystems, diverse ecosystems, conservation and global ecology.

Practicals: The course involves four practical exercises.
Evaluation: A written final exam 80%, practical reports 20%. Students need to pass both components (minimum grade 50/100).

Undergraduate biology students are not allowed to take this course

Lectures: Mendelian inheritance. Sex chromosomes. Cytoplasmic inheritance. Chromosomes. Cell division (mitosis and meiosis). Life cycles. Linkage and recombination in eukaryotes. Bacterial genetics. Gene mapping and tetrad analysis. Genotype and phenotype. Chromosomal changes. DNA: Structure and replication. RNA: Transcription. Rgulation of gene transcription. Gene isolation and manipulation. Genomics. Transposons.  Mutations. Repair and recombination.  Model organisms. Laboratory work: : I. The fruitfly Drosophila melanogaster. II. Mitosis in onions. III. Plasmids and restriction enzymes. IV. PCR. V. Analysis of asci from Sordaria fimicola.

Exam: Laboratory and problems 25%, written 75%. Minimum mark needed for each part.

Course description: The fundamental concepts of calculus will be discussed. Subjects: Limits and continuous functions. Differentiable functions, rules for derivatives, derivatives of higher order, antiderivatives. Applications of differential calculus: Extremal value problems, linear approximation. The main functions in calculus: logarithms, exponential functions and trigonometric functions. The mean value theorem. Integration: The definite integral and rules of integration. The fundamental theorem of calculus. Techniques of integration, improper integrals. Series and sequences. Ordinary differential equations. Vectors and matrix calculations.

This course focuses on the structure of the periodic table and properties of the elements based on their place in the periodic table. The students learn about the naturally occurring forms of the elements, isolation of the elements and common chemical reactions. Atomic theory is taught as a base for understanding the properties of the elements and their reactivity. Early theories of the structure of the hydrogen atome put forward by Bohr and their development to modern view of the atom structure are covered. The electronic structure of the atom is described, and theories describing formation of chemical bonds such as valence bond theory, VSEPR, and molecular orbital theory are used to determine structures and predict reactivity of molecules. Processes for purification of metals from their naturally occurring ores is covered as well as properties of metalloids and nonmetals. The transition metal elements, and the formation of coordination compounds with solubility, equilibria, ions and electron pair donors will be introduced. Radioactivity, formation and types of radioactive species, reactions and their applications will be introduced.

Standardization of a pipette. Quantitative determinations of Ni in steel, Ca in milk, Na in water and wine.  Quantitative analysis of acetic acid and hydrogenperoxide. Identification of amino acid. Quantitative analysis of fluoride using electochemical cells.  Two component analysis using photometry.

During this course, students will be introduced to organisms and acellular entities too small to be seen by the unaided eye.  They can acquire knowledge on the characteristics of bacteria, archaea, viruses and eukaryotic microorganisms.  The course will explain the importance of microorganisms, how they live in diverse and dynamic ecosystems and how some affect humans, for example by being valuable for the food industry or by causing disease.  The students will gain laboratory experience and practice aseptic techniques. 

Evolutionary biology: Darwin and evolution of the evolutionary theory. The tree of life, natural selection and adaptation.  How evolution works: The origin of variation, the raw material for evolution.  The genetical theory of natural selection. Evolution of phenotypic traits.  Genetic drift: Evolution at random and in space. Species and speciation. Products of evolution:  Conflict and cooperation. Life-history evolution. Coevolution among species. Evolution of genes and genomes. Evolution and development. Macroevolution and the history of life: Phylogeny, the history of life, geography of evolution and the evolution of biological diversity. Evolution above the species level. Human evolution and human society.

At the beginning of the course some main statistical concepts are introduced, such as population, sample, variable and randomness. Various descriptive statistics are introduced, as well as basic graphical representations. Fundamentals of probability theory are introduced, as well as the most common probability distributions. The rest of the course deals with inferential statistics where hypotheses tests and confidence intervals for means, variance and proportions are covered as well a analysis of variance (ANOVA) and simple linear regression. Students will learn how to apply the above mentioned methods in the statistical software R.

Organic chemistry appears all around us, both in the biological aspects of our world and in the production aspect of many of our daily products. Organic chemistry also appears in many other subjects, such as biochemistry, pharmaceutical science, food science, and medicine. Understanding of the organic chemistry can help deepen our understanding of  production processes in the chemical and food industry, biochemical pathways, and the manufacturing and bioactivity of drugs.

In this course, we will cover the basics of organic chemistry. We will cover the various functional groups, their properties and reactivity, with a special emphasis on alkanes, alkenes, alkynes, alkyl halides, and aromatic compounds. We will also cover stereochemistry of organic compounds and their analysis and identification using NMR, IR, and MS.

Many of the compounds we use in our daily lives (plastics, medicine, glue and more) are produced via organic chemistry. The pharmaceutical industry is a good example of where it is important to be able to synthesize the right products, isolate/purify them and identify whether the correct product was synthesized. In this course, students will be trained in the main laboratory techniques of organic chemistry and can be beneficial in the chemical industry. Students will also receive training in analyzing their results and writing scientific reports.

Content of course: Energy and the first law of thermodynamics. Chemical thermodynamics. Entropy and the second law of thermodynamics. The third  law of thermodynamics. Free energy. Phase equilibrium. Solutions, in particular ionic solutions. Chemical equilibrium. Electrochemistry. Transport processes: gas kinetics, diffusion and heat transport. Mechanism and rate of chemical reactions. Enzyme catalysis.

Text book:  Atkins' Physical Chemistry 11th Edition

A thorough treatment of the fundamentals of biochemistry - part one; structure and function of macromolecules. The scope of biochemistry. Water and its properties. Interactions in biomolecules. Amino acids, peptides and the structure of proteins. Protein function.  Protein stability, folding, and dynamics related to function. Carbohydrates and glycobiology. Lipids, membranes and membrane proteins. Enzyme kinetics, regulation of enzyme activity, and mechanisms of enzyme catalysis. Signal transduction and membrane receptors. Structure of nucleic acids, stability, and basic recombinant technology. Final grade is combined from the final exam (85% ) and a midterm exam (15%).

Lectures:
Twice weekly (2 x 40 min.) Probelm solving class (2 x 40 min.) weekly.

Course evaluation:
Final exam (3 hours): 85% of final grade.
Midterm: 15% of final grade.

Textbook:
Nelson D.L. & Cox M.M. Lehninger: Principles of Biochemistry, 8th Edition, 2021

The cell biology part includes four lectures each week for 14 weeks (4L week for 14 weeks). The content includes: Introduction to cell biology, structure and evolution of eukaryotic cells. The main emphasis is on eukaryotic cells. Chemistry of the cell and energy conversion, structure and function of cellular macromolecules. The structure and function of cellular organs and functional units like the cell membrane, nucleus, mitochondria, chloroplasts, cytoskeleton, golgi-system, lysosomes and peroxisomes. Intracellular regulation and signal pathways linked to communication between cells, together with cell differentiation and cancer. Details on extracellular matrix are included and basic immunology.

Histology is an independent short course accompanying the LÍF315G cell biology course. The course is structured as a practical course with support lectures, and lectures and practical exercises last for 6 weeks. The practical classes are primarily based on examining histological samples under a microscope and generating properly annotated histological sketches. Attendance is mandatory in practical lessons. The final exam is held two weeks after the last lecture.

The aim of the course is to introduce the basics of histology and tissue structure, as well as to make students independent in the use of microscopes when examining tissue samples. The lectures discuss the properties of individual tissues, the characteristics and function of different cell types and the properties of the extracellular matrix in a tissue-specific context. The preparation of samples is also discussed separately.

Content of course: Principles of quantum mechanics. Chemical bonds. Intermolecular- interactions. Relationship between quantum chemistry and spectroscopy. Spectroscopic methods. Spectral analysis. Introduction to laboratory exercises.

Experiments: Solution calorimeter. Enthalpy of combustion (bomb calorimeter). Phase diagrams and distillation of liquid solutions. Chemical equilibrium and solubility derived from conductivity measurements. Reaction kinetics (rate equations). Electrolyte solutions. Heat of vaporization. Viscosity. Spectroscopy of organic dyes. Chemical equilibrium by spectroscopic methods. Fluorescence of micellar solution. NMR spectroscopy.

Alcohols and phenols, ethers and epoxides, aldehydes and ketones, carboxylic acids, derivatives carbanions, amines, carbohydrates, amino acids and proteins. Spectroscopical identification of organic compounds.

Laboratory work: Synthesis and analytical organic chemistry.

The course is a practical course with weekly supportive lectures.  The lectures provide heroretical background of the instrumental methods and the instruments. The supportive lectures are part of lab exercises and attendance is compulsory.

The students learn about modern methods and instruments used in analytical chemistry based on interaction between chemical- and physical properties of the substances and the electromagnetic field. Chromatographic methods used to separate mixtures into single pure compounds will be introduced.  The focus of the course is the analysis of organic compounds.

Laboratory work: Fluorimetry, atomic absorption, spectrophotometry and applications of IR, UV and visible and NMR spectroscopy. Gas- and liquid (HPLC) chromatography. Gas chromatography/mass spectrometry (GC/MS).

In this course, the main metabolic processes of cells are studied, with a focus on carbohydrate, fat, and protein metabolism, as well as the metabolic regulation of these processes. The course begins with a detailed examination of carbohydrate metabolism, including glycolysis (both aerobic and anaerobic), the citric acid cycle, and the pentose phosphate pathway. Then we continue into pathways such as gluconeogenesis, glycogen breakdown, and then into how carbohydrate metabolism is regulated.

Next, the focus shifts to fat metabolism, where the breakdown of triglycerides, fatty acid oxidation, and fatty acid synthesis are explained. Special emphasis is placed on the regulation of fat metabolism and the control of enzymes involved in these processes. Following this, protein metabolism is addressed, where protein hydrolysis, amino acid degradation, and the urea cycle are studied.

The course also covers the integration and regulation of metabolic pathways, with a focus on the complex regulation that occurs in the key steps of these pathways, considering both intracellular signals and hormones. It examines how these processes adapt to various conditions to maintain homeostasis and the effects of disruptions in their regulation. Lastly, photosynthesis and the Calvin cycle are covered.

This course is highly beneficial for those seeking an in-depth understanding of biochemical processes and the biochemistry of the human body.

Lectures are held twice a week (2 x 40 minutes) over 13-14 weeks. 

This course combines weekly laboratory sessions (6 hours per week for 12–13 weeks) with weekly lectures (2×40 minutes per week for 13–14 weeks).

Lectures provide the theoretical background for the laboratory work and introduce practical applications of the concepts covered.

In the laboratory, students will gain hands-on experience with core techniquesand safety precautions in biochemical research, including:

• Methods for protein purification.
• Quantitative analysis of proteins and specific chemical groups.
• Assessment of protein stability and the effects of ligands.
• Measurement of enzyme kinetics and the effects of inhibitors.
• Use of biochemical databases and related software for research and data interpretation.
• Processing numerical data and the use of linear and nonlinear models on experimental data.
• Proper use of a laboratory notebook and accurate recording of experimental data.
• Writing scientific reports based on experimental findings.

This course provides an introduction to the principles and applications of applied biotechnology, with an emphasis on its role in industry and society. Biotechnology is inherently interdisciplinary, combining elements of molecular biology, chemistry, engineering, and pharmaceutical sciences. Through lectures, group projects, student presentations, and guest seminars, students will explore how biotechnology products and processes are developed — from laboratory research to industrial implementation.

The course is organized around five major areas of applied biotechnology: (1) pharmaceutical biotechnology, (2) Industrial biotechnology in the chemical and food sectors, (3) Clinical biotechnology, (4) Natural product discovery and purification and (5) energy and environmental biotechnology.

This course is based on lectures, project work, student presentations and discussions. One field trip to a biotech company will be done.

The course is co-taught with ILT102F - Introduction to Applied Biotechnology. It is not possible to take both courses.

The course is divided into lectures, practical sessions, discussions and student projects.

Lectures: Theoretical basis of common molecular-biology techniques and their application in research. Course material provided by teachers.

Laboratory practice in molecular biology techniques: Training in general molecular biology laboratory skills and active documentation in laboratory notebooks.

Discussions are associated with all other parts (lectures, practicals and student projects)

Main topics:  Laboratory notebooks, electronic laboratory notebooks and standard operating procedures (SOP's), use of online tools. Basics of DNA work and DNA cloning. Plasmids and plasmid maps, working with DNA sequences. DNA and RNA isolation and quantification (Southern and Northern blotting, PCR, RT-PCR, qRT-PCR), restriction enzymes, DNA sequencing techniques and data analysis. Basics of E. coli cultures and plasmid work. Basics of cell culture and transfection. Model organisms: E.coli, S. cerevisiae, C. reinhardtii, A. thaliana, C. elegans, D. melanogaster, M. musculus.  Transgenesis and genetic tools in bacteria, yeast and multicellular organisms. CRISPR technique and gRNA design. RNA interference and other methods for conditional gene expression and inhibition. Protein expression and analysis. How to raise and use antibodies for research. Western blot, immunostaining of cells and tissues, radioactive techniques. Microscopy in molecular biology. Methods used in recent research papers will be discussed.

Student projects: Study of a recent method or method group. Output varies by year but aims at training students in reference work and different approaches to mediating scientific material. Examples include: Posters, Essays, Talks, Videos, Webpages and Podcasts.

The main purpose of this course is to teach the principles of chemical structure and bonding. The main focus will be on using symmetry and group theory in constructing molecular orbitals for simple molecules and ions. VSEPR and VB methods will also be used to study bonding and structure of molecules. The crystalline solid state, formulas, structures and properties. Each students performance in two interm exams will count as 20% of the final grade. The assignments will count as 5% of the final grade

Generation of carbanions and their reactions, such as alkylation of enolates, C vs. O alkylation, aldol condensation and acylation of carbons. Decarboxylation and formation of double bonds will also be covered, along with organometallic chemistry. General and specific laboratory techniques of synthesis and analysis and the use of databases (Scifinder). Spectroscopic identification of all compounds. 75% of homework must be turned in in order to be allowed to take the exam.

The students will be trained to work independently in the laboratory, which serves as preparation for research projects in graduate school or on the job. Instead of standard and well-tested protocols, like found in most undergraduate laboratory classes, general descriptions from books or journal articles will be used. Each student gets his own four-step synthesis project. The students will carry out the reactions, monitor their progress and isolate the products while documenting their work in their notebooks. They will solve problems that may come up while performing their experiments, including optimization of reaction conditions if the reactions don´t work as expected the first time around. The structures of the products will be verified by spectroscopic methods, in particular NMR.

The students will be shown how to find reaction conditions in journal articles using databases (Scifinder). The lectures will also cover how results are communicated in scientific journals. The students will write an article describing their synthetic work, instead of writing reports for each step. A template from Organic Letters will be used.

The synthesis projects are based on the material covered in EFN511G, where the theme is formation of C-C bonds, for example by alkylation of 1,3-dicarbonyl compounds, by the use of the Wittig and Grignard reactions, aldol condensations etc.

Third year students can elect to work on a specialized 15 ECTS laboratory project under the auspices of a member of the teaching staff depending on availability. The main advisor and the location of the project can be outside the faculty of sciences. If so, a member of staff is responsible for all practical matters. The aim is for the student to gain experience in carrying out research from an initial idea and to a final written report. This will generally give the student the opportunity to gain some new technical skills.
The research project concludes with a report which is graded by the supervisor with consensus from another member of staff. Reports must conform to the format and rules of the Faculty of Physical Sciences.

Lectures: Mendelian genetics, organization of the human genome, structure of chromosomes, chromosomal changes and syndromes, gene mapping via association and whole genome sequencing methods, genetic analysis, genetic screening, genetics of simple and complex traits, genes and environment, cancer genetics, gene therapy, human and primate evolution, ethical issues concerning human genetics, informed consent and private information. Students are expected to have prior knowledge of the principles genetics.

Practical: Analyses of genetic data, study of chromosomal labelling, analyses of genetic associations and transcriptomes.

Note: Only one course of either TÖL101G Tölvunarfræði 1 or TÖL105G Tölvunarfræði 1a can count towards the BS degree.

The Java programming language is used to introduce basic concepts in computer programming: Expressions and statements, textual and numeric data types, conditions and loops, arrays, methods, classes and objects, input and output. Programming and debugging skills are practiced in quizzes and projects throughout the semester.

The immune system, organs and cells. Innate immunity, phagocytes, complement, inflammation. Adaptive immunity, development and differentiation of lymphocytes. Specificity and antigen recognition, function of B- and T-cells. Immune responses, immunological memory, mucosal immunity. Immunological tolerance and immune regulation. Immune deficiency, hypersensitivity, autoimmunity and transplantation.  Treatment and intervention of autoimmune and allergic diseases.  Vaccination and protection from infections. Immunological methods and diagnostics. Students presentations and discussions of scientific articles under the teachers supervision.

Subject Matter: Newtonian Mechanics for particles and rigid bodies. Dynamical variables and conservation laws. Elements of Fluid Mechanics. Thermodynamics. Elements of Electromagnetism. Laboratory exercises in which students are trained in handling physical instruments, performing measurements and interpreting the data.

The course is thaught in English or Icelandic according to the needs of the students.

The aim of this course is to introduce different applications of microorganisms and to help students develop independent research skills. In the first part of the course, students will visit a geothermal area and subsequently work on a research project where they isolate, identify and study bacterial strains.

The second part will introduce different fields of microbial biotechnology and how they have been shaped by recent progress in microbiology, molecular biology and biochemistry. State of the art will be covered regarding subjects such as microbial diversity as a resource of enzymes and biocompounds; bioprospecting, thermophiles, marine microbes and microalgae, biorefineries (emphasis on seaweed and lignocellulose), enzymes (emphasis on carbohydrate active enzymes), metabolic engineering (genetic engineering, omics), energy-biotechnology, cultivation and fermentation technology. The course will exemplify Icelandic biotechnology where applicable. Cultivation/production technology and yeast will be presented specifically in practical sessions in the brewing of beer.

The third part will cover environmental sampling, microbial communities and biofilms, microbes in aquatic and terrestrial environments, indoor air quality and the impact of molds. Also, water- and food-borne pathogens, risk assessment and surveillance, water treatment, microbial remediation, methane production and global warming. Students will visit waste management and water treatment plants and review and present selected research articles.

Additional teaching one Saturday in end of September or beginning of October.

Programming in Python (for computations in engineering and science): Main commands and statements (computations, control statements, in- and output), definition and execution of functions, datatypes (numbers, matrices, strings, logical values, records), operations and built-in functions, array and matrix computation, file processing, statistics, graphics. Object-oriented programming: classes, objects, constructors and methods. Concepts associated with design and construction of program systems: Programming environment and practices, design and documentation of function and subroutine libraries, debugging and testing of programmes.

The characteristics of protein structures at the different structural levels. How structure determines the different properties of proteins. Structural classes of proteins and their characteristics. Relationship between molecular structure and biological function. Interactions that determine structural stability of proteins. Protein folding and unfolding. Effects of different parameters, e.g. temperature, pH, salts and denaturants on protein stability. Techniques used for determination structure and different properties proteins. Selected topics in protein structure function relationships.

Course plan: Lectures twice per week (2x40 min. each time). Computer lab once per week (2x40 min.). Lab sessions involve training using the WWW to study proteins. Tutorials and practice of using SwissPDBviewer program for solving specific assignments related to topics covered in lectures.

This course focuses on methodology and recent innovations in biochemistry, emphasizing both analytical and computational techniques. It is divided into several modules, each taught by experts in their respective fields. While lectures form the core of the material, additional resources such as articles or book chapters may be assigned when appropriate. Practical demonstrations of research equipment may also be included. Students are expected to submit several assignments throughout the semester.

The course will explore recent research in various specialized areas of biochemistry, and the content of the modules is regularly updated.

Topics covered may include single-molecule spectroscopy, protein mass spectrometry, structural biochemistry, binding affinity and thermodynamics and computational biochemistry.

Lectures: Homeostasis, membrane potentials, neurons, nervous systems, endocrinology, sensory physiology, muscles, circulation, respiration, osmoregulation and excretion, digestion, metabolism, energy balance, reproduction.

Lab work: 1) Membrane potentials and ligands. 2) Somatic nerves/skeletal muscle. 3) Ergometry.
Other assignments: Online exams and review questions, information will be given at the beginning of the course.

Developmental biology unifies multiple subject areas within life- and medical sciences and many fundamental discoveries on molecular and cellular processes come from developmental biology research. The aim of the course is for students to gain broad overview of the main topics of developmental biology and to acquire knowledge of the fundamental aspects of the development of different groups of vertebrates and invertebrates at multiple levels, ranging from the whole organism to the role of molecules in regulating developmental processes.

Main lecture topics: The role of development. Historical overview. Development of unicellular organisms. Reproduction and genetic recombination. Developmental patterns among multicellular animals. Specification and determination of embryonic cell fates. Modern techniques in developmental biology. Controlling gene expression, - developmental genes. Importance of cell interactions. Structure of gametes, fertilization and activation of the egg. Early stages of development in selected invertebrates. Specification of embryonic axes and organs of the fruit fly, -a hierarchical system of gene control. Early stages of development and specification of embryonic axes in amphibias, birds and mammals. Fate of embryonic layers and organogensis in vertebrates. Limb formation in tetrapods. Sex determination, sexual development and development of gametes among invertebrates and vertebrates. Plant development.

In the practical exercises, the aim of the course is for students to gain training and skills in the handling and microscopic analysis of embryos, while also strengthening their knowledge of the main developmental events in different animal groups. Emphasis is also placed on students gaining practice in the use of databases in developmental genetics and genetics.

Practicals: The use of databases and genome browsers; Drosophila embryonic development and metamorphosis; zebrafish development; chick development.

Student presentations: Sudents are required to give two short presentations on course-related topics. The grade for each presentation represents 10% of the total grade for the course. Minimum grade required is 5,0 for both presentations.

Third year students can elect to work on a specialized 15 ECTS laboratory project under the auspices of a member of the teaching staff depending on availability. The main advisor and the location of the project can be outside the faculty of sciences. If so, a member of staff is responsible for all practical matters. The aim is for the student to gain experience in carrying out research from an initial idea and to a final written report. This will generally give the student the opportunity to gain some new technical skills.
The research project concludes with a report which is graded by the supervisor with consensus from another member of staff. Reports must conform to the format and rules of the Faculty of Physical Sciences.

The emphasis is on research articles. Resent research in various field with links to cell biology are included but can vary between years. For each lecture max three research articles are included.

Each student gives a seminar on one research article with details on methods and results. The students write a report (essay) on the article and discusses the results in a critical way.

Examples of topics included in the course: innate immunity, prions, the proteins pontin and reptin, polarized epithelium, development of trachea, data analyses and gene expression, autophagy, the origin of the nucleus.

Lectures: The molecular basis of life (chemical bonds, biological molecules, structure of DNA, RNA and proteins). Genomes and the flow of biological information. Chromosome structure and function, chromatin and nucleosomes. The cell cycle, DNA replication. Chromosome segregaition, Transcription. Regulation of transcription. RNA processing. Translation. Regulation of translation. Regulatory RNAs. Protein modification and targeting. DNA damage, checkpoints and DNA repair mechanisms. Repair of DNA double-strand breaks and homologous recombination. Mobile DNA elements. Tools and techniques in molecular Biology, including Model organisms.

Seminar: Students present and discuss selected research papers and hand in a short essay.

Laboratory work: Work on molecular genetics project relevant to current research. Basic methods such as gene cloning, gene transfer and expression, PCR, sequencing, DNA isolation and restriction analysis, electrophoresis of DNA and proteins will be used.

Exam: Laboratory 10%, seminar 15%, written final exam 75%.

The immune system, organs and cells. Innate immunity, phagocytes, complement, inflammation. Adaptive immunity, development and differentiation of lymphocytes. Specificity and antigen recognition, function of B- and T-cells. Immune responses, immunological memory, mucosal immunity. Immunological tolerance and immune regulation. Immune deficiency, hypersensitivity, autoimmunity and transplantation.  Treatment and intervention of autoimmune and allergic diseases.  Vaccination and protection from infections. Immunological methods and diagnostics. Students presentations and discussions of scientific articles under the teachers supervision.

Medicine, biology, biochemistry, food- and nutrition, and related fields.

The basis of the atomic theory. Stoichiometry. Types of chemical reactions and solution stoichiometry. Properties of gases. Chemical equilibrium. Acids and bases. Applications of aqueous equilibria. Chemical thermodynamics. Enthropy, free energy and equilibrium. Electrochemistry. Chemical kinetics. Physical properties of solutions.

Molar volume of gases, thermochemistry, reaction enthalpies and Hesse's law, Rate of chemical reactions, decomposition of hydrogen peroxide, reaction reversibility and Le Chatelier's principle, determination of acid ionization constants, oxidation-reduction; electrochemistry, thermodynamics of an electrochemical cell.

Lectures:
I. Introduction: The study of life; major themes and approaches.

II. The evolution of life: Basis of ideas on evolution and the tree of life. Classification of organisms, major groups,their characteristics and evolutionary history, covering viruses, prokaryotes and eukaryotes, protists, fungi, algae, plants, invertebrates and vertebrates.

III. Structure and function of plants and animals: Plants; structure and growth, vascular systems, photosynthesis, nutrients and reproduction. Animals (emphasis on vertebrates); structure and major tissues of the body, nutrition and digestion, signalling systems of hormones, vascular systems and respiration, excretory- and reproductive systems, development, nervous system and movements, sensory systems.

IV. Ecology: The major biomes of the earth and the distribution of organisms, behavioural ecology, population ecology, structure and dynamics of communities and ecosystems, diverse ecosystems, conservation and global ecology.

Practicals: The course involves four practical exercises.
Evaluation: A written final exam 80%, practical reports 20%. Students need to pass both components (minimum grade 50/100).

Undergraduate biology students are not allowed to take this course

Lectures: Mendelian inheritance. Sex chromosomes. Cytoplasmic inheritance. Chromosomes. Cell division (mitosis and meiosis). Life cycles. Linkage and recombination in eukaryotes. Bacterial genetics. Gene mapping and tetrad analysis. Genotype and phenotype. Chromosomal changes. DNA: Structure and replication. RNA: Transcription. Rgulation of gene transcription. Gene isolation and manipulation. Genomics. Transposons.  Mutations. Repair and recombination.  Model organisms. Laboratory work: : I. The fruitfly Drosophila melanogaster. II. Mitosis in onions. III. Plasmids and restriction enzymes. IV. PCR. V. Analysis of asci from Sordaria fimicola.

Exam: Laboratory and problems 25%, written 75%. Minimum mark needed for each part.

Course description: The fundamental concepts of calculus will be discussed. Subjects: Limits and continuous functions. Differentiable functions, rules for derivatives, derivatives of higher order, antiderivatives. Applications of differential calculus: Extremal value problems, linear approximation. The main functions in calculus: logarithms, exponential functions and trigonometric functions. The mean value theorem. Integration: The definite integral and rules of integration. The fundamental theorem of calculus. Techniques of integration, improper integrals. Series and sequences. Ordinary differential equations. Vectors and matrix calculations.

This course focuses on the structure of the periodic table and properties of the elements based on their place in the periodic table. The students learn about the naturally occurring forms of the elements, isolation of the elements and common chemical reactions. Atomic theory is taught as a base for understanding the properties of the elements and their reactivity. Early theories of the structure of the hydrogen atome put forward by Bohr and their development to modern view of the atom structure are covered. The electronic structure of the atom is described, and theories describing formation of chemical bonds such as valence bond theory, VSEPR, and molecular orbital theory are used to determine structures and predict reactivity of molecules. Processes for purification of metals from their naturally occurring ores is covered as well as properties of metalloids and nonmetals. The transition metal elements, and the formation of coordination compounds with solubility, equilibria, ions and electron pair donors will be introduced. Radioactivity, formation and types of radioactive species, reactions and their applications will be introduced.

Standardization of a pipette. Quantitative determinations of Ni in steel, Ca in milk, Na in water and wine.  Quantitative analysis of acetic acid and hydrogenperoxide. Identification of amino acid. Quantitative analysis of fluoride using electochemical cells.  Two component analysis using photometry.

During this course, students will be introduced to organisms and acellular entities too small to be seen by the unaided eye.  They can acquire knowledge on the characteristics of bacteria, archaea, viruses and eukaryotic microorganisms.  The course will explain the importance of microorganisms, how they live in diverse and dynamic ecosystems and how some affect humans, for example by being valuable for the food industry or by causing disease.  The students will gain laboratory experience and practice aseptic techniques. 

Evolutionary biology: Darwin and evolution of the evolutionary theory. The tree of life, natural selection and adaptation.  How evolution works: The origin of variation, the raw material for evolution.  The genetical theory of natural selection. Evolution of phenotypic traits.  Genetic drift: Evolution at random and in space. Species and speciation. Products of evolution:  Conflict and cooperation. Life-history evolution. Coevolution among species. Evolution of genes and genomes. Evolution and development. Macroevolution and the history of life: Phylogeny, the history of life, geography of evolution and the evolution of biological diversity. Evolution above the species level. Human evolution and human society.

At the beginning of the course some main statistical concepts are introduced, such as population, sample, variable and randomness. Various descriptive statistics are introduced, as well as basic graphical representations. Fundamentals of probability theory are introduced, as well as the most common probability distributions. The rest of the course deals with inferential statistics where hypotheses tests and confidence intervals for means, variance and proportions are covered as well a analysis of variance (ANOVA) and simple linear regression. Students will learn how to apply the above mentioned methods in the statistical software R.

Organic chemistry appears all around us, both in the biological aspects of our world and in the production aspect of many of our daily products. Organic chemistry also appears in many other subjects, such as biochemistry, pharmaceutical science, food science, and medicine. Understanding of the organic chemistry can help deepen our understanding of  production processes in the chemical and food industry, biochemical pathways, and the manufacturing and bioactivity of drugs.

In this course, we will cover the basics of organic chemistry. We will cover the various functional groups, their properties and reactivity, with a special emphasis on alkanes, alkenes, alkynes, alkyl halides, and aromatic compounds. We will also cover stereochemistry of organic compounds and their analysis and identification using NMR, IR, and MS.

Many of the compounds we use in our daily lives (plastics, medicine, glue and more) are produced via organic chemistry. The pharmaceutical industry is a good example of where it is important to be able to synthesize the right products, isolate/purify them and identify whether the correct product was synthesized. In this course, students will be trained in the main laboratory techniques of organic chemistry and can be beneficial in the chemical industry. Students will also receive training in analyzing their results and writing scientific reports.

Content of course: Energy and the first law of thermodynamics. Chemical thermodynamics. Entropy and the second law of thermodynamics. The third  law of thermodynamics. Free energy. Phase equilibrium. Solutions, in particular ionic solutions. Chemical equilibrium. Electrochemistry. Transport processes: gas kinetics, diffusion and heat transport. Mechanism and rate of chemical reactions. Enzyme catalysis.

Text book:  Atkins' Physical Chemistry 11th Edition

A thorough treatment of the fundamentals of biochemistry - part one; structure and function of macromolecules. The scope of biochemistry. Water and its properties. Interactions in biomolecules. Amino acids, peptides and the structure of proteins. Protein function.  Protein stability, folding, and dynamics related to function. Carbohydrates and glycobiology. Lipids, membranes and membrane proteins. Enzyme kinetics, regulation of enzyme activity, and mechanisms of enzyme catalysis. Signal transduction and membrane receptors. Structure of nucleic acids, stability, and basic recombinant technology. Final grade is combined from the final exam (85% ) and a midterm exam (15%).

Lectures:
Twice weekly (2 x 40 min.) Probelm solving class (2 x 40 min.) weekly.

Course evaluation:
Final exam (3 hours): 85% of final grade.
Midterm: 15% of final grade.

Textbook:
Nelson D.L. & Cox M.M. Lehninger: Principles of Biochemistry, 8th Edition, 2021

The cell biology part includes four lectures each week for 14 weeks (4L week for 14 weeks). The content includes: Introduction to cell biology, structure and evolution of eukaryotic cells. The main emphasis is on eukaryotic cells. Chemistry of the cell and energy conversion, structure and function of cellular macromolecules. The structure and function of cellular organs and functional units like the cell membrane, nucleus, mitochondria, chloroplasts, cytoskeleton, golgi-system, lysosomes and peroxisomes. Intracellular regulation and signal pathways linked to communication between cells, together with cell differentiation and cancer. Details on extracellular matrix are included and basic immunology.

Histology is an independent short course accompanying the LÍF315G cell biology course. The course is structured as a practical course with support lectures, and lectures and practical exercises last for 6 weeks. The practical classes are primarily based on examining histological samples under a microscope and generating properly annotated histological sketches. Attendance is mandatory in practical lessons. The final exam is held two weeks after the last lecture.

The aim of the course is to introduce the basics of histology and tissue structure, as well as to make students independent in the use of microscopes when examining tissue samples. The lectures discuss the properties of individual tissues, the characteristics and function of different cell types and the properties of the extracellular matrix in a tissue-specific context. The preparation of samples is also discussed separately.

Content of course: Principles of quantum mechanics. Chemical bonds. Intermolecular- interactions. Relationship between quantum chemistry and spectroscopy. Spectroscopic methods. Spectral analysis. Introduction to laboratory exercises.

Experiments: Solution calorimeter. Enthalpy of combustion (bomb calorimeter). Phase diagrams and distillation of liquid solutions. Chemical equilibrium and solubility derived from conductivity measurements. Reaction kinetics (rate equations). Electrolyte solutions. Heat of vaporization. Viscosity. Spectroscopy of organic dyes. Chemical equilibrium by spectroscopic methods. Fluorescence of micellar solution. NMR spectroscopy.

Alcohols and phenols, ethers and epoxides, aldehydes and ketones, carboxylic acids, derivatives carbanions, amines, carbohydrates, amino acids and proteins. Spectroscopical identification of organic compounds.

Laboratory work: Synthesis and analytical organic chemistry.

The course is a practical course with weekly supportive lectures.  The lectures provide heroretical background of the instrumental methods and the instruments. The supportive lectures are part of lab exercises and attendance is compulsory.

The students learn about modern methods and instruments used in analytical chemistry based on interaction between chemical- and physical properties of the substances and the electromagnetic field. Chromatographic methods used to separate mixtures into single pure compounds will be introduced.  The focus of the course is the analysis of organic compounds.

Laboratory work: Fluorimetry, atomic absorption, spectrophotometry and applications of IR, UV and visible and NMR spectroscopy. Gas- and liquid (HPLC) chromatography. Gas chromatography/mass spectrometry (GC/MS).

In this course, the main metabolic processes of cells are studied, with a focus on carbohydrate, fat, and protein metabolism, as well as the metabolic regulation of these processes. The course begins with a detailed examination of carbohydrate metabolism, including glycolysis (both aerobic and anaerobic), the citric acid cycle, and the pentose phosphate pathway. Then we continue into pathways such as gluconeogenesis, glycogen breakdown, and then into how carbohydrate metabolism is regulated.

Next, the focus shifts to fat metabolism, where the breakdown of triglycerides, fatty acid oxidation, and fatty acid synthesis are explained. Special emphasis is placed on the regulation of fat metabolism and the control of enzymes involved in these processes. Following this, protein metabolism is addressed, where protein hydrolysis, amino acid degradation, and the urea cycle are studied.

The course also covers the integration and regulation of metabolic pathways, with a focus on the complex regulation that occurs in the key steps of these pathways, considering both intracellular signals and hormones. It examines how these processes adapt to various conditions to maintain homeostasis and the effects of disruptions in their regulation. Lastly, photosynthesis and the Calvin cycle are covered.

This course is highly beneficial for those seeking an in-depth understanding of biochemical processes and the biochemistry of the human body.

Lectures are held twice a week (2 x 40 minutes) over 13-14 weeks. 

This course combines weekly laboratory sessions (6 hours per week for 12–13 weeks) with weekly lectures (2×40 minutes per week for 13–14 weeks).

Lectures provide the theoretical background for the laboratory work and introduce practical applications of the concepts covered.

In the laboratory, students will gain hands-on experience with core techniquesand safety precautions in biochemical research, including:

• Methods for protein purification.
• Quantitative analysis of proteins and specific chemical groups.
• Assessment of protein stability and the effects of ligands.
• Measurement of enzyme kinetics and the effects of inhibitors.
• Use of biochemical databases and related software for research and data interpretation.
• Processing numerical data and the use of linear and nonlinear models on experimental data.
• Proper use of a laboratory notebook and accurate recording of experimental data.
• Writing scientific reports based on experimental findings.

This course provides an introduction to the principles and applications of applied biotechnology, with an emphasis on its role in industry and society. Biotechnology is inherently interdisciplinary, combining elements of molecular biology, chemistry, engineering, and pharmaceutical sciences. Through lectures, group projects, student presentations, and guest seminars, students will explore how biotechnology products and processes are developed — from laboratory research to industrial implementation.

The course is organized around five major areas of applied biotechnology: (1) pharmaceutical biotechnology, (2) Industrial biotechnology in the chemical and food sectors, (3) Clinical biotechnology, (4) Natural product discovery and purification and (5) energy and environmental biotechnology.

This course is based on lectures, project work, student presentations and discussions. One field trip to a biotech company will be done.

The course is co-taught with ILT102F - Introduction to Applied Biotechnology. It is not possible to take both courses.

The course is divided into lectures, practical sessions, discussions and student projects.

Lectures: Theoretical basis of common molecular-biology techniques and their application in research. Course material provided by teachers.

Laboratory practice in molecular biology techniques: Training in general molecular biology laboratory skills and active documentation in laboratory notebooks.

Discussions are associated with all other parts (lectures, practicals and student projects)

Main topics:  Laboratory notebooks, electronic laboratory notebooks and standard operating procedures (SOP's), use of online tools. Basics of DNA work and DNA cloning. Plasmids and plasmid maps, working with DNA sequences. DNA and RNA isolation and quantification (Southern and Northern blotting, PCR, RT-PCR, qRT-PCR), restriction enzymes, DNA sequencing techniques and data analysis. Basics of E. coli cultures and plasmid work. Basics of cell culture and transfection. Model organisms: E.coli, S. cerevisiae, C. reinhardtii, A. thaliana, C. elegans, D. melanogaster, M. musculus.  Transgenesis and genetic tools in bacteria, yeast and multicellular organisms. CRISPR technique and gRNA design. RNA interference and other methods for conditional gene expression and inhibition. Protein expression and analysis. How to raise and use antibodies for research. Western blot, immunostaining of cells and tissues, radioactive techniques. Microscopy in molecular biology. Methods used in recent research papers will be discussed.

Student projects: Study of a recent method or method group. Output varies by year but aims at training students in reference work and different approaches to mediating scientific material. Examples include: Posters, Essays, Talks, Videos, Webpages and Podcasts.

The main purpose of this course is to teach the principles of chemical structure and bonding. The main focus will be on using symmetry and group theory in constructing molecular orbitals for simple molecules and ions. VSEPR and VB methods will also be used to study bonding and structure of molecules. The crystalline solid state, formulas, structures and properties. Each students performance in two interm exams will count as 20% of the final grade. The assignments will count as 5% of the final grade

Generation of carbanions and their reactions, such as alkylation of enolates, C vs. O alkylation, aldol condensation and acylation of carbons. Decarboxylation and formation of double bonds will also be covered, along with organometallic chemistry. General and specific laboratory techniques of synthesis and analysis and the use of databases (Scifinder). Spectroscopic identification of all compounds. 75% of homework must be turned in in order to be allowed to take the exam.

The students will be trained to work independently in the laboratory, which serves as preparation for research projects in graduate school or on the job. Instead of standard and well-tested protocols, like found in most undergraduate laboratory classes, general descriptions from books or journal articles will be used. Each student gets his own four-step synthesis project. The students will carry out the reactions, monitor their progress and isolate the products while documenting their work in their notebooks. They will solve problems that may come up while performing their experiments, including optimization of reaction conditions if the reactions don´t work as expected the first time around. The structures of the products will be verified by spectroscopic methods, in particular NMR.

The students will be shown how to find reaction conditions in journal articles using databases (Scifinder). The lectures will also cover how results are communicated in scientific journals. The students will write an article describing their synthetic work, instead of writing reports for each step. A template from Organic Letters will be used.

The synthesis projects are based on the material covered in EFN511G, where the theme is formation of C-C bonds, for example by alkylation of 1,3-dicarbonyl compounds, by the use of the Wittig and Grignard reactions, aldol condensations etc.

Third year students can elect to work on a specialized 15 ECTS laboratory project under the auspices of a member of the teaching staff depending on availability. The main advisor and the location of the project can be outside the faculty of sciences. If so, a member of staff is responsible for all practical matters. The aim is for the student to gain experience in carrying out research from an initial idea and to a final written report. This will generally give the student the opportunity to gain some new technical skills.
The research project concludes with a report which is graded by the supervisor with consensus from another member of staff. Reports must conform to the format and rules of the Faculty of Physical Sciences.

Lectures: Mendelian genetics, organization of the human genome, structure of chromosomes, chromosomal changes and syndromes, gene mapping via association and whole genome sequencing methods, genetic analysis, genetic screening, genetics of simple and complex traits, genes and environment, cancer genetics, gene therapy, human and primate evolution, ethical issues concerning human genetics, informed consent and private information. Students are expected to have prior knowledge of the principles genetics.

Practical: Analyses of genetic data, study of chromosomal labelling, analyses of genetic associations and transcriptomes.

Note: Only one course of either TÖL101G Tölvunarfræði 1 or TÖL105G Tölvunarfræði 1a can count towards the BS degree.

The Java programming language is used to introduce basic concepts in computer programming: Expressions and statements, textual and numeric data types, conditions and loops, arrays, methods, classes and objects, input and output. Programming and debugging skills are practiced in quizzes and projects throughout the semester.

The immune system, organs and cells. Innate immunity, phagocytes, complement, inflammation. Adaptive immunity, development and differentiation of lymphocytes. Specificity and antigen recognition, function of B- and T-cells. Immune responses, immunological memory, mucosal immunity. Immunological tolerance and immune regulation. Immune deficiency, hypersensitivity, autoimmunity and transplantation.  Treatment and intervention of autoimmune and allergic diseases.  Vaccination and protection from infections. Immunological methods and diagnostics. Students presentations and discussions of scientific articles under the teachers supervision.

Subject Matter: Newtonian Mechanics for particles and rigid bodies. Dynamical variables and conservation laws. Elements of Fluid Mechanics. Thermodynamics. Elements of Electromagnetism. Laboratory exercises in which students are trained in handling physical instruments, performing measurements and interpreting the data.

The course is thaught in English or Icelandic according to the needs of the students.

The aim of this course is to introduce different applications of microorganisms and to help students develop independent research skills. In the first part of the course, students will visit a geothermal area and subsequently work on a research project where they isolate, identify and study bacterial strains.

The second part will introduce different fields of microbial biotechnology and how they have been shaped by recent progress in microbiology, molecular biology and biochemistry. State of the art will be covered regarding subjects such as microbial diversity as a resource of enzymes and biocompounds; bioprospecting, thermophiles, marine microbes and microalgae, biorefineries (emphasis on seaweed and lignocellulose), enzymes (emphasis on carbohydrate active enzymes), metabolic engineering (genetic engineering, omics), energy-biotechnology, cultivation and fermentation technology. The course will exemplify Icelandic biotechnology where applicable. Cultivation/production technology and yeast will be presented specifically in practical sessions in the brewing of beer.

The third part will cover environmental sampling, microbial communities and biofilms, microbes in aquatic and terrestrial environments, indoor air quality and the impact of molds. Also, water- and food-borne pathogens, risk assessment and surveillance, water treatment, microbial remediation, methane production and global warming. Students will visit waste management and water treatment plants and review and present selected research articles.

Additional teaching one Saturday in end of September or beginning of October.

Programming in Python (for computations in engineering and science): Main commands and statements (computations, control statements, in- and output), definition and execution of functions, datatypes (numbers, matrices, strings, logical values, records), operations and built-in functions, array and matrix computation, file processing, statistics, graphics. Object-oriented programming: classes, objects, constructors and methods. Concepts associated with design and construction of program systems: Programming environment and practices, design and documentation of function and subroutine libraries, debugging and testing of programmes.

The characteristics of protein structures at the different structural levels. How structure determines the different properties of proteins. Structural classes of proteins and their characteristics. Relationship between molecular structure and biological function. Interactions that determine structural stability of proteins. Protein folding and unfolding. Effects of different parameters, e.g. temperature, pH, salts and denaturants on protein stability. Techniques used for determination structure and different properties proteins. Selected topics in protein structure function relationships.

Course plan: Lectures twice per week (2x40 min. each time). Computer lab once per week (2x40 min.). Lab sessions involve training using the WWW to study proteins. Tutorials and practice of using SwissPDBviewer program for solving specific assignments related to topics covered in lectures.

This course focuses on methodology and recent innovations in biochemistry, emphasizing both analytical and computational techniques. It is divided into several modules, each taught by experts in their respective fields. While lectures form the core of the material, additional resources such as articles or book chapters may be assigned when appropriate. Practical demonstrations of research equipment may also be included. Students are expected to submit several assignments throughout the semester.

The course will explore recent research in various specialized areas of biochemistry, and the content of the modules is regularly updated.

Topics covered may include single-molecule spectroscopy, protein mass spectrometry, structural biochemistry, binding affinity and thermodynamics and computational biochemistry.

Lectures: Homeostasis, membrane potentials, neurons, nervous systems, endocrinology, sensory physiology, muscles, circulation, respiration, osmoregulation and excretion, digestion, metabolism, energy balance, reproduction.

Lab work: 1) Membrane potentials and ligands. 2) Somatic nerves/skeletal muscle. 3) Ergometry.
Other assignments: Online exams and review questions, information will be given at the beginning of the course.

Developmental biology unifies multiple subject areas within life- and medical sciences and many fundamental discoveries on molecular and cellular processes come from developmental biology research. The aim of the course is for students to gain broad overview of the main topics of developmental biology and to acquire knowledge of the fundamental aspects of the development of different groups of vertebrates and invertebrates at multiple levels, ranging from the whole organism to the role of molecules in regulating developmental processes.

Main lecture topics: The role of development. Historical overview. Development of unicellular organisms. Reproduction and genetic recombination. Developmental patterns among multicellular animals. Specification and determination of embryonic cell fates. Modern techniques in developmental biology. Controlling gene expression, - developmental genes. Importance of cell interactions. Structure of gametes, fertilization and activation of the egg. Early stages of development in selected invertebrates. Specification of embryonic axes and organs of the fruit fly, -a hierarchical system of gene control. Early stages of development and specification of embryonic axes in amphibias, birds and mammals. Fate of embryonic layers and organogensis in vertebrates. Limb formation in tetrapods. Sex determination, sexual development and development of gametes among invertebrates and vertebrates. Plant development.

In the practical exercises, the aim of the course is for students to gain training and skills in the handling and microscopic analysis of embryos, while also strengthening their knowledge of the main developmental events in different animal groups. Emphasis is also placed on students gaining practice in the use of databases in developmental genetics and genetics.

Practicals: The use of databases and genome browsers; Drosophila embryonic development and metamorphosis; zebrafish development; chick development.

Student presentations: Sudents are required to give two short presentations on course-related topics. The grade for each presentation represents 10% of the total grade for the course. Minimum grade required is 5,0 for both presentations.

Third year students can elect to work on a specialized 15 ECTS laboratory project under the auspices of a member of the teaching staff depending on availability. The main advisor and the location of the project can be outside the faculty of sciences. If so, a member of staff is responsible for all practical matters. The aim is for the student to gain experience in carrying out research from an initial idea and to a final written report. This will generally give the student the opportunity to gain some new technical skills.
The research project concludes with a report which is graded by the supervisor with consensus from another member of staff. Reports must conform to the format and rules of the Faculty of Physical Sciences.

The emphasis is on research articles. Resent research in various field with links to cell biology are included but can vary between years. For each lecture max three research articles are included.

Each student gives a seminar on one research article with details on methods and results. The students write a report (essay) on the article and discusses the results in a critical way.

Examples of topics included in the course: innate immunity, prions, the proteins pontin and reptin, polarized epithelium, development of trachea, data analyses and gene expression, autophagy, the origin of the nucleus.

Lectures: The molecular basis of life (chemical bonds, biological molecules, structure of DNA, RNA and proteins). Genomes and the flow of biological information. Chromosome structure and function, chromatin and nucleosomes. The cell cycle, DNA replication. Chromosome segregaition, Transcription. Regulation of transcription. RNA processing. Translation. Regulation of translation. Regulatory RNAs. Protein modification and targeting. DNA damage, checkpoints and DNA repair mechanisms. Repair of DNA double-strand breaks and homologous recombination. Mobile DNA elements. Tools and techniques in molecular Biology, including Model organisms.

Seminar: Students present and discuss selected research papers and hand in a short essay.

Laboratory work: Work on molecular genetics project relevant to current research. Basic methods such as gene cloning, gene transfer and expression, PCR, sequencing, DNA isolation and restriction analysis, electrophoresis of DNA and proteins will be used.

Exam: Laboratory 10%, seminar 15%, written final exam 75%.

The immune system, organs and cells. Innate immunity, phagocytes, complement, inflammation. Adaptive immunity, development and differentiation of lymphocytes. Specificity and antigen recognition, function of B- and T-cells. Immune responses, immunological memory, mucosal immunity. Immunological tolerance and immune regulation. Immune deficiency, hypersensitivity, autoimmunity and transplantation.  Treatment and intervention of autoimmune and allergic diseases.  Vaccination and protection from infections. Immunological methods and diagnostics. Students presentations and discussions of scientific articles under the teachers supervision.

Medicine, biology, biochemistry, food- and nutrition, and related fields.