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 mechanisms of cellular peptide/protein synthesis and degradation, major principles that govern protein folding and structure, and explain the fundamental connection between structure and function of proteins
• describe different strategies and methods for the chemical synthesis of peptides and for the production, isolation, structure determination, functional analysis and modification of proteins
• experimentally isolate and crystallize proteins as well as determine their basic physico-chemical and functional properties
• analyse and interpret protein sequences and structures and use such information to predict protein function
• describe how proteins can be used for production and development of drugs, for biotechnological and other industrial and scientific purposes, and explain how this is facilitated by knowledge of the structure and function of proteins
• write a report in the form of a scientific article

Content

Production and degradation: Biological and recombinant protein synthesis. Biological and chemical peptide synthesis. Post-translational and chemical modifications. Genetic engineering and directed evolution. Protein degradation.

Protein structure, function and bioinformatics: Folding. Structure determination by X-ray crystallography, NMR spectroscopy and cryo-electron microscopy. Structure modelling and analysis using molecular graphics. Protein-ligand, protein-DNA and protein-protein interactions. Kinetic and thermodynamic characterisation of interactions. Examples for proteins: Enzymes, membrane proteins, structural proteins, DNA-binding regulatory proteins. Structure-function relationships. Introduction to databases for protein sequences, structures and functions and to protein bioinformatics tools and methods.

Applications: Examples for biotechnological, medical and scientific use of proteins.

Practical and theoretical lab projects: Expression, purification, characterisation of an enzyme (the results of this project are presented in a report formed as a scientific publication). Protein crystallisation.

Instruction

The course is given in form of lectures as well as experimental and theoretical exercises and projects. Exercises and projects are compulsory and carried out individually or in groups.

Assessment

Experimental and theoretical exercises and projects (5 credits) are examined during the course. One of the reports should have a method section in English that meets the requirements set for publication in international journals in biochemistry. An overall written examination (5 credits) is given at the end of the course. The final grade for the course is given as a weighted average grade for all assessed parts.

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 directives

Cannot be included in a degree together with the course Structure and function of proteins 10 credits (1KB403).