Entry requirements

One of the following is required: (1) 60 credits of which at least 40 credits in chemistry including 10 credits in organic chemistry and 5 credits in biochemistry, or (2) 60 credits of which at least 40 credits in biology, together with 10 credits in organic chemistry and 5 credits in biochemistry, or (3) 60 credits within the Teacher Education Programme of which at least 30 credits in chemistry including 10 credits in organic chemistry and 5 credits in biochemistry.

Learning outcomes

After the course the student should be able to

• account for the undergoing molecular mechanisms of biological processes
• account for basic concept within kinetics of enzyme-catalysed one- and two-substrate reactions
• explain structure/function relationships in enzyme-catalysed reactions as well as for the most common cofactors
• describe and discuss regulatory principles of enzyme activity
• account for molecular genetic processes such as replication, transcription and translation and their regulation
• explain principles for energy transformation and biosynthesis in cellular systems and reflect on their regulation
• plan and carry out correctly biochemical experiments including enzyme characterisation with the most essential biochemical analysis and purification methods.

Content

Chemical structure and molecular organisation of biological systems. Supramolecular complexes, organelles. Molecular dynamics in living cells: Bioenergetics and intermediary metabolism. Regulation of the metabolism on transcription and protein level. Photosynthesis.

The structure and evolution of proteins. Protein ligand and protein-protein interactions. Allosteric enzymes, cooperativity. Covalent modification, partial proteolysis. Signal substances, receptors, signal amplification. Biochemical toxicology. Enzyme kinetics. Enzyme mechanisms, cofactors. Definition of primary-, secondary- and tertiary structure. Functional domains and multienzyme complexes. Immunoglobulins and immunological analysis. Design of protein function.

Membrane topology and membrane transport, chemiosmotic coupling. Oxidative phosphorylation, photo phosphorylation, electron transport.

DNA as major source of information. Gene structure. Expression of genetic information: Regulation of transcription, operons, induction, repression, transcription factors, protein-DNA interactions. Mutations, oncogenes, cancer. Biosynthesis of immunoglobulins, alternative splicing. Biosynthesis of proteins, ribosomes. Post-translational modification and intracellular distribution of proteins. Basic hybrid-DNA technique.

Experimental methodology: Analytical and preparative separation methods. Using computers for visualisation and modelling of macromolecules, experimental data analysis and bioinformatics are integrated in various parts of the course.

In the course, integrated communication training with feedback and self-assessment occurs.

Instruction

The course is given in the form of lectures, discussions, exercises and laboratory sessions.

Assessment

Written examinations correspond to 9 HE credits. The laboratory sessions correspond to 6 HE credits. The final grade corresponds to a weighted average of the results of the written examination and the laboratory sessions.

Other directives

Cannot be included in a degree together with the courses Biochemistry 15 credits (1KB402) or Biochemistry II 15 credits (1KB411). Participation in laboratory sessions and exercises is compulsory.