C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2023
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2022
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
autumn 2021
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2020
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2019
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2016
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2015
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2014
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
Study Materials
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2013
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
Study Materials
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2012
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is english. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
Study Materials
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2011
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Prerequisites
NOW(C8875)
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 11 fields of study the course is directly associated with, display
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is english. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
Study Materials
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2010
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Prerequisites
NOW(C8875)
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 10 fields of study the course is directly associated with, display
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is english. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
Study Materials
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2009
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Timetable
Tue 10:00–10:50 C04/211
Prerequisites
NOW(C8875)
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 10 fields of study the course is directly associated with, display
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is english. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Study of interactions between proteins and DNA

Faculty of Science
Autumn 2008
Extent and Intensity
1/0/0. 4 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Timetable
Thu 10:00–10:50 C04/211
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 15 fields of study the course is directly associated with, display
Course objectives
1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Assessment methods
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Further Comments
Study Materials
The course is taught annually.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Study of interactions between proteins and DNA

Faculty of Science
Autumn 2007
Extent and Intensity
1/0/0. 2 credit(s) (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 15 fields of study the course is directly associated with, display
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Language of instruction
English
Further Comments
Study Materials
The course is taught annually.
The course is taught every week.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Study of interactions between proteins and DNA

Faculty of Science
Autumn 2006
Extent and Intensity
1/0/0. (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Timetable
Thu 13:00–13:50 C04/211
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 15 fields of study the course is directly associated with, display
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Language of instruction
English
Further Comments
Study Materials
The course is taught annually.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2024

The course is not taught in Autumn 2024

Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2018

The course is not taught in Autumn 2018

Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
Course is no more offered.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
autumn 2017

The course is not taught in autumn 2017

Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assembly, and folding; Mad cow and other diseases; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, environment and hormone responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosylation). 4) DNA-protein interactions, types of interaction motifs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pull-down). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is English. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will also have to deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
Course is no more offered.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Study of interactions between proteins and DNA

Faculty of Science
Spring 2007

The course is not taught in Spring 2007

Extent and Intensity
1/0/0. (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 15 fields of study the course is directly associated with, display
Language of instruction
English
Further Comments
The course is taught annually.
The course is taught every week.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2011 - acreditation

The information about the term Autumn 2011 - acreditation is not made public

Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Prerequisites
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 10 fields of study the course is directly associated with, display
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is english. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Protein Preparation and Characterization III - Protein-mediated interactions

Faculty of Science
Autumn 2010 - only for the accreditation
Extent and Intensity
1/0/0. 1 credit(s) (plus 2 credits for an exam). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Prerequisites
NOW(C8875)
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 10 fields of study the course is directly associated with, display
Course objectives
The main aim of the course is to discuss the role of protein-mediated interactions in the biology of the cell. At the end of the course students should be able to understand and explain protein-ligand, protein-protein and protein-DNA interactions and motifs responsible for such interactions will be presented in the context of their biological significance. The course will also include theory of individual methods used for study of protein-mediated interactions.
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Literature
  • MEYERS., Robert A. Encyclopedia of Molecular Cell Biology and Molecular Medicine, 2nd Edition. 2004. ISBN 3-527-30545-9. info
  • BRANDEN, Carl and John TOOZE. Introduction to Protein Structure. 1991. ISBN 0-8153-0270-3. info
Teaching methods
The course will be taken in block during the semester. The teaching language is english. Each lecture will consist of summary of previous lecture, actual lecture and case examples. Special focus will be given for group discussions.
Assessment methods
The course will be ended by test. Each student will have to also deliver home assignment that describes their particular project with the potential implementation of the methods and techniques discussed during the course.
Language of instruction
English
Follow-Up Courses
Further Comments
The course is taught annually.
The course is taught in blocks.
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.

C8857 Study of interactions between proteins and DNA

Faculty of Science
Autumn 2007 - for the purpose of the accreditation
Extent and Intensity
1/0/0. (fasci plus compl plus > 4). Type of Completion: zk (examination).
Teacher(s)
doc. Mgr. Lumír Krejčí, Ph.D. (lecturer)
Guaranteed by
doc. Mgr. Lumír Krejčí, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Course Enrolment Limitations
The course is also offered to the students of the fields other than those the course is directly associated with.
fields of study / plans the course is directly associated with
there are 15 fields of study the course is directly associated with, display
Syllabus
  • 1) General concept DNA RNA PROTEIN; Proteins - their structure, assmebly, and folding; Mad cow and other disease; Domains and motifs; Predictions. 2) Why and how do the proteins interact; Little bit of Math; Data mining; Protein localization (NLS), membrane transport , transport in cytosol etc.); Role of protein interactions (cell cycle, enviroment and hormon responses). 3) Modification of protein interactions, their role and types (phosphorylation, Ubq, Sumo, glycosilation, 4) DNA-protein interactions, types of interaction motivs, their roles (replication, transcription, repair), modification again 5) Methods of study (microscopy, Y2H, FRET, in vitro /pulldow). 6) Methods II (IP,CHIP, far western, EMSA, Biocore etc.). 7) Single protein versus complex of proteins. 8) Examples: DNA repair mechanisms, from single protein to multi-protein complexes. 9) DNA repair II
Language of instruction
English
Further Comments
The course is taught annually.
The course is taught every week.
The course is also listed under the following terms Autumn 2010 - only for the accreditation, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023.
  • Enrolment Statistics (recent)