Biochemistry II

15 credits

Syllabus, Bachelor's level, 1KB411

A revised version of the syllabus is available.
Code
1KB411
Education cycle
First cycle
Main field(s) of study and in-depth level
Biology G1F, Chemistry G1F
Grading system
Pass with distinction (5), Pass with credit (4), Pass (3), Fail (U)
Finalised by
The Faculty Board of Science and Technology, 18 March 2010
Responsible department
Department of Chemistry - BMC

Entry requirements

Organic Chemistry I, 10 credits and Biochemistry I, 5 credits or Chemistry of the Cell, 5 credits or equivalent courses.

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

- account for simpler structure/function relationships in enzyme-catalysed reactions

- account for simpler structure/function relationships fort the most common cofactors.

- account for regulatory principles of enzyme activity

- account for molecular genetic processes such as replication, transcription and translation and regulation of these

- account for principles for energy transformation and biosynthesis in cellular systems and regulation of these.

- 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.

Instruction

The course is given in the form of lectures, discussions, exercises and laboratory sessions. Participation in laboratory sessions and exercises is compulsory. In the course, integrated communication training with feedback and self-assessment occurs.

Assessment

Written examinations are organised at the end of the course and/or during the time of the course and correspond to 9 HE credits. The laboratory sessions correspond to 6 HE credits. To pass final grades it is required that all parts have been assessed passed. The final grade corresponds to a weighted average of the results of the written examination and the laboratory sessions.

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