On completion of the course, the student should be able to:
describe different strategies and methods for the production, isolation, structure determination, functional analysis and modification of proteins
produce peptides and proteins and 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
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 and NMR spectroscopy. 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, 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.
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. Peptide synthesis.
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.
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 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.