PřF:Bi7410 Protein Engineering - Course Information
Bi7410 Protein Engineering
Faculty of ScienceSpring 2020
- Extent and Intensity
- 1/0/0. 1 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
- Teacher(s)
- doc. Mgr. Radka Chaloupková, Ph.D. (lecturer)
doc. Mgr. David Bednář, Ph.D. (lecturer)
prof. Mgr. Jiří Damborský, Dr. (lecturer) - Guaranteed by
- prof. Mgr. Jiří Damborský, Dr.
Department of Experimental Biology – Biology Section – Faculty of Science
Contact Person: doc. Mgr. Radka Chaloupková, Ph.D.
Supplier department: Department of Experimental Biology – Biology Section – Faculty of Science - Timetable
- Thu 16:00–17:50 B11/333
- Course Enrolment Limitations
- The course is offered to students of any study field.
- Course objectives
- The aim of this course is to introduce methods and strategies commonly used in protein engineering to improve catalytic properties of enzymes.
- Learning outcomes
- At the end of the course, students will be able to:
- understand principles and explain differences between rational design, directed evolution, and semi-rational design;
- prepare the design of a protein engineering strategy with the aim to improve properties of studied protein;
- get a general knowledge about searches of novel genes/proteins in bioinformatics databases;
- explain the principles of methods of isolation, expression, and purification of proteins;
- explain principles and select a biophysical method suitable for analysis of secondary, tertiary and quaternary structure of proteins;
- describe the various screening techniques used for selection and/or screening of novel protein variants with improved properties - Syllabus
- 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.
- Literature
- recommended literature
- Protein engineering handbook. Edited by Stefan Lutz - Uwe Bornscheuer. Weinheim: Wiley-VCH, 2009, xli, 409-9. ISBN 9783527318506. info
- not specified
- 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
- Teaching methods
- Lectures, class discussion.
- Assessment methods
- 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
- Czech
- Further comments (probably available only in Czech)
- Study Materials
The course is taught annually.
General note: Předmět se doporučuje zapsat v 2. nebo 4. semestru.
- Enrolment Statistics (Spring 2020, recent)
- Permalink: https://is.muni.cz/course/sci/spring2020/Bi7410