Entry requirements

One of the following is required: (1) 60 credits of which at least 40 credits in chemistry including 15 credits in biochemistry, or (2) 60 credits of which at least 40 credits in biology, and 15 credits in biochemistry.

Learning outcomes

On completion of the course, the student should be able to:

• describe and compare biological and chemical processes for peptide/protein synthesis, modification and degradation,
• describe biological and artificial protein evolution,
• describe, motivate choice of, and use methods for production, purification and analysis of proteins,
• explain principles of protein folding, and account for protein structures as well as biomolecular interactions and structure-function relationships,
• explain the principles of enzyme catalysis, various catalytic and regulatory mechanisms, and the methods used to study them,
• apply methods for protein structure determination and computational modelling as well as analysis of protein sequences and structures,
• analyse protein sequences and structures and use this information to predict the properties of proteins,
• explain how proteins are used as drug targets or can function as therapeutics, through various forms of oral and written communication.

Content

Protein synthesis and degradation: Native and recombinant protein and peptide synthesis. Chemical peptide synthesis. Post‑translational and chemical modifications of proteins. Protein degradation. Biological and artificial protein evolution.

Protein structure, function, and bioinformatics: Protein folding and structure determination. Analysis of physicochemical properties, three‑dimensional structures, and protein–protein interactions using experimental methods (X‑ray crystallography, NMR, Cryo‑EM). Modelling, prediction, and visualization of protein structures using computational methods. Examples of different classes of proteins (enzymes, membrane proteins, structural proteins, DNA‑binding regulatory proteins). Structure–function relationships. Introduction to databases for protein sequences, structures, and functions, as well as web‑based tools for protein bioinformatics and structural analysis.

Enzymes: Principles of enzyme catalysis and analysis of enzyme function and kinetic properties.

Applications: Use of proteins in research and industrial development. Proteins as drug targets and proteins as therapeutics.

Laboratory work and theoretical projects: Strategies for protein production. Biotechnological production and biochemical characterization of an enzyme. Protein crystallization. Graphical visualization of protein structures. Bioinformatics. Investigation and presentation of the biochemical mechanism of action of a given drug.

Instruction

Teaching is conducted through lectures, seminars, theoretical projects, and laboratory exercises. Laboratory work and projects are carried out both individually and in groups.

Assessment

Laboratory work and theoretical projects (7 credits) are assessed through written and oral examinations during the course. A comprehensive written examination (8 credits) is given at the end of the course.

If there are special reasons for doing so, an examiner may make an exception from the method of assessment indicated and allow a student to be assessed by another method. An example of special reasons might be a certificate regarding special pedagogical support from the disability coordinator of the university.

Other regulations

Cannot be included in a degree together with the course Structure and funciton of proteins (1KB403, 1KB422) and Proteins and drugs (1KB404, 1KB423).