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 artifical processes for peptide/protein synthesis, modification and degradation,
• describe natural and directed protein evolution, 
• describe, motivate choice of, and use methods for production, purification and analysis of proteins, 
• explain principles of protein structure and folding, biomolecular interactions and structure-function relationships, 
• apply methods for protein structure determination and computational modelling and analysis of protein sequences and structures,
• analyse protein sequences and structures and use such information to predict the properties of proteins,
• account for protein functions and applications, including protein-based drug discovery and protein-based biopharmaceuticals using various types of presentation techniques.

Content

Production and degradation: Native and recombinant protein and peptide synthesis. Chemical peptide synthesis. Post-translational and chemical modifications. Natural protein evolution, genetic engineering and targeted evolution. Protein degradation. 

Protein structure, function and bioinformatics: Protein folding and structural determination. Analysis of the physicochemical properties, three-dimensional structures and interactions of proteins using experimental methods (X-ray crystallography, NMR, Cryo-EM) and computational methods. Examples of important proteins families: 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 analyses.

Applications: Use of proteins in biotechnological and medical research and development. Protein-based drug development strategies, proteins as drugs.

Practical and theoretical lab projects: Biotechnological and biochemical techniques to produce and characterize an enzyme. Protein crystallization.

Studies of how a given drug works at the biochemical level.

Instruction

Lectures, laboratory work, theoretical exercises and project. Exercises and project are performed individually or in group.

Assessment

Experimental and theoretical exercises and project (7 credits) during the course. A final written exam (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).