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.
  • Enrolment Statistics (Autumn 2014, recent)
  • Permalink: https://is.muni.cz/course/sci/autumn2014/C8857