The course is offered to students of any study field.
The aim of this course is to introduce methods and strategies commonly used in protein engineering.
At the end of the course, students should be able to understand and explain differences between rational design and directed evolution, and have a general knowledge about miscellaneous topics such as searches in bioinformatics databases, isolation, expression or purification of novel proteins. Students will also get an overview of several biophysical techniques used for analysis of secondary, tertiary and quaternary structure, as well as of screening methods used for selection of novel protein variants with improved properties.
1. Protein synthesis, protein structure, protein function and structure-function relationships.
2. Identification of putative enzymes in sequence databases, bioinformatic analysis.
3. Isolation of genes from host organisms, cloning, preparation of recombinant proteins, host organisms, protein expression and protein purification.
4. Structural characterization of proteins, an overview of spectroscopic techniques for the analysis of protein secondary and tertiary structure; an overview of techniques for analysis of protein quaternary structure.
5. Enzymes, enzyme catalysis, factors influencing the speed of enzymatic reaction.
6. Enzyme applications, targets of protein engineering, protein engineering approaches, advantages and limitations.
7. Rational design, prediction of the structure of enzyme variant, evaluation of the effect of mutations on enzyme structure and function.
8. Directed evolution, screening of mutants.
9. Examples of application of protein engineering to improve enzyme catalytic efficiency.
10. Examples of application of protein engineering to improve enzyme stability.
11. Examples of application of protein engineering to improve enzyme enantioselectivity.
Protein engineering handbook. Edited by Stefan Lutz - Uwe Bornscheuer. Weinheim: Wiley-VCH, 2009. xli, 409-9. ISBN 9783527318506. info
Directed evolution library creation : methods and protocols. Edited by Frances Hamilton Arnold - George Georgiou. Totowa, N.J.: Humana Press, 2003. x, 224. ISBN 1588292851. info
FERSHT, Alan. Structure and mechanism in protein science :a guide to enzyme catalysis and protein folding. New York: W.H. Freeman, 1998. xxi, 631 s. ISBN 0-7167-3268-8. info
Lectures, class discussion.
Final written test consists of 25 questions and is scored on a 25-point scale. A minimum score of 13 is required to successfully pass the exam.
Language of instruction
The course is taught annually.
The course is taught: every week.