Bi7410 Protein Engineering

Faculty of Science
Spring 2021
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)
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
Mon 1. 3. to Fri 14. 5. Thu 16:00–17:50 online_B2
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.
The course is also listed under the following terms spring 2012 - acreditation, Spring 2013, Spring 2014, Spring 2015, Spring 2016, Spring 2017, spring 2018, Spring 2019, Spring 2020, Spring 2022.
  • Enrolment Statistics (recent)
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