Bi7410 Protein Engineering

Faculty of Science
Spring 2025
Extent and Intensity
2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
In-person direct teaching
Teacher(s)
Mgr. Michal Vašina, Ph.D. (lecturer)
doc. Mgr. David Bednář, Ph.D. (lecturer)
Guaranteed by
prof. Mgr. Jiří Damborský, Dr.
Department of Experimental Biology – Biology Section – Faculty of Science
Contact Person: Mgr. Michal Vašina, Ph.D.
Supplier department: Department of Experimental Biology – Biology Section – Faculty of Science
Timetable
Mon 17. 2. to Sat 24. 5. Tue 14:00–15:50 B11/333
Prerequisites
Basic knowledge of biochemistry and molecular biology.
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 applications, targets of protein engineering, protein biosynthesis, protein structure and 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, protein sample quality control.
  • 4. Functional and structural characterization of proteins, protein interactions, enzyme catalysis, factors influencing the speed of enzymatic reaction, an overview of techniques for the analysis of protein secondary, tertiary structure and quaternary structure.
  • 5. Protein engineering approaches, advantages and limitations, overview of mutagenesis techniques.
  • 6. Directed evolution, screening and selection of mutants.
  • 7. In silico mutagenesis and semi-rational design.
  • 8. Rational design, prediction of the structure of enzyme variant, evaluation of the effect of mutations on enzyme structure and function.
  • 9. Examples of application of protein engineering: Directed evolution.
  • 10. Examples of application of protein engineering: Rational design.
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 2021, Spring 2022, Spring 2024, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2026
Extent and Intensity
2/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
In-person direct teaching
Teacher(s)
Mgr. Michal Vašina, 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: Mgr. Michal Vašina, Ph.D.
Supplier department: Department of Experimental Biology – Biology Section – Faculty of Science
Prerequisites
Basic knowledge of biochemistry and molecular biology.
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 applications, targets of protein engineering, protein biosynthesis, protein structure and 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, protein sample quality control.
  • 4. Functional and structural characterization of proteins, protein interactions, enzyme catalysis, factors influencing the speed of enzymatic reaction, an overview of techniques for the analysis of protein secondary, tertiary structure and quaternary structure.
  • 5. Protein engineering approaches, advantages and limitations, overview of mutagenesis techniques.
  • 6. Directed evolution, screening and selection of mutants.
  • 7. In silico mutagenesis and semi-rational design.
  • 8. Rational design, prediction of the structure of enzyme variant, evaluation of the effect of mutations on enzyme structure and function.
  • 9. Examples of application of protein engineering: Directed evolution.
  • 10. Examples of application of protein engineering: Rational design.
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)
The course is taught annually.
The course is taught every week.
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 2021, Spring 2022, Spring 2024, Spring 2025.

Bi7410 Protein Engineering

Faculty of Science
Spring 2024
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
Mon 19. 2. to Sun 26. 5. Tue 14:00–15:50 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.
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 2021, Spring 2022, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2022
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
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.
The course is taught every week.
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 2021, Spring 2024, Spring 2025, Spring 2026.

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)
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
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, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 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.
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 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2019
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)
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 18. 2. to Fri 17. 5. 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.
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.
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
Study Materials
The course is taught annually.
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 2020, Spring 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
spring 2018
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)
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 B11/305
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.
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.
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
Study Materials
The course is taught annually.
The course is also listed under the following terms spring 2012 - acreditation, Spring 2013, Spring 2014, Spring 2015, Spring 2016, Spring 2017, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2017
Extent and Intensity
1/0. 1 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Radka Chaloupková, Ph.D. (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 20. 2. to Mon 22. 5. Thu 16:00–17:50 B11/235
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.
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.
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
Study Materials
The course is taught annually.
The course is also listed under the following terms spring 2012 - acreditation, Spring 2013, Spring 2014, Spring 2015, Spring 2016, spring 2018, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2016
Extent and Intensity
1/0. 1 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Radka Chaloupková, Ph.D. (lecturer)
Mgr. Jan Brezovský, Ph.D. (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 B11/235
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.
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.
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
Study Materials
The course is taught annually.
The course is also listed under the following terms spring 2012 - acreditation, Spring 2013, Spring 2014, Spring 2015, Spring 2017, spring 2018, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2015
Extent and Intensity
1/0. 1 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Radka Chaloupková, Ph.D. (lecturer)
Mgr. Jan Brezovský, Ph.D. (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 B11/235
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.
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.
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
Study Materials
The course is taught annually.
The course is also listed under the following terms spring 2012 - acreditation, Spring 2013, Spring 2014, Spring 2016, Spring 2017, spring 2018, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2014
Extent and Intensity
1/0. 1 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Radka Chaloupková, Ph.D. (lecturer)
Mgr. Eva Šebestová, Ph.D. (lecturer)
Mgr. Jan Brezovský, Ph.D. (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 16:00–17:50 B11/235
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.
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.
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
Study Materials
The course is taught annually.
The course is also listed under the following terms spring 2012 - acreditation, Spring 2013, Spring 2015, Spring 2016, Spring 2017, spring 2018, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2013
Extent and Intensity
1/0. 1 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Radka Chaloupková, Ph.D. (lecturer)
Mgr. Eva Šebestová, Ph.D. (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 17:00–17:50 C13/332
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.
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.
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
3 written tests + final written test
Language of instruction
Czech
Further Comments
Study Materials
The course is taught annually.
The course is also listed under the following terms spring 2012 - acreditation, Spring 2014, Spring 2015, Spring 2016, Spring 2017, spring 2018, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2023

The course is not taught in Spring 2023

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
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)
The course is taught annually.
The course is taught every week.
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 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
Spring 2012

The course is not taught in Spring 2012

Extent and Intensity
1/0. 1 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Radka Chaloupková, Ph.D. (lecturer)
Mgr. Eva Šebestová, Ph.D. (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
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.
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.
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
3 written tests + final written test
Language of instruction
Czech
Further Comments
The course is taught annually.
The course is taught every week.
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 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.

Bi7410 Protein Engineering

Faculty of Science
spring 2012 - acreditation

The information about the term spring 2012 - acreditation is not made public

Extent and Intensity
1/0. 1 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Radka Chaloupková, Ph.D. (lecturer)
Mgr. Eva Šebestová, Ph.D. (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
Course Enrolment Limitations
The course is offered to students of any study field.
Course objectives (in Czech)
Během kurzu získají studenti základní přehled o metodách proteinového inženýrství a biofyzikálních technikách využívaných ke strukturní a funkční charakterizaci nově upravených proteinových variant. Na základě záskaných informací by studenti měli porozumět dvěma základním přístupů proteinového inženýrství, racionálnímu designu a řízené evoluci, a umět rozhodnout za jakých podmínek lze daný přístup proteinového inženýrství použít. Studenti by dále měli získat přehled o bioinformatických nástrojích používaných pro identifikaci nových putativních enzymů v genomových databázích, o izolaci příslušných genů z hostitelských organismů a metodách exprese a purifikace rekombinantních proteinů. Na konci kurzu by studenti měli být schopni rozhodnut jakou metodu použít pro selekci pozitivních enzymových variant s konkrétní vylepšenou vlastností z připravených mutantních knihoven a rovněž vybrat nejvhodnější biofyzikální techniku pro charakterizaci správného strukturního uspořádání, termostability a aktivity enzymů.
Syllabus (in Czech)
  • 1.Proteosyntéza, struktura proteinů, funkce proteinů, strukturně-funkční vztahy
  • 2.Identifikace putativních enzymů v genomových databázích - bioinformatická analýza
  • 3.Izolace genů z hostitelských organismů, klonování, příprava rekombinantních proteinů, přehled hostitelský organismů, exprese proteinů
  • 4. Purifikace proteinů – přehled chromatografických technik
  • 5. Strukturní charakterizace proteinů – přehled spektroskopických technik pro analýzu sekundární a terciální struktury proteinů
  • 6. Analýza kvarterní struktury proteinů
  • 7. Enzymy, enzymová katalýza, faktory ovlivňující rychlost enzymových reakcí
  • 8. Aplikační využití enzymů, strategie proteinového inženýrství
  • 9. Racionální design – předpověď struktury mutantního enzymů, hodnocení efektu mutace na strukturu a funkci enzymů
  • 10. Molekulárně biologické metody proteinového inženýrství
  • 11. Řízená evoluce, screening mutantních variant
  • 12. Příklady využití proteinového inženýrství pro vylepšení katalytické účinnosti a stability enzymů
Teaching methods (in Czech)
Přednášky-teoretická příprava, diskuze aktuálního tématu
Assessment methods (in Czech)
Písemná zkouška
Language of instruction
Czech
Further Comments
The course is taught annually.
The course is taught every week.
The course is also listed under the following terms Spring 2013, Spring 2014, Spring 2015, Spring 2016, Spring 2017, spring 2018, Spring 2019, Spring 2020, Spring 2021, Spring 2022, Spring 2024, Spring 2025, Spring 2026.
  • Enrolment Statistics (recent)