C3210 Structural bioinformatics

Faculty of Science
autumn 2021
Extent and Intensity
1/0/0. 1 credit(s) (plus extra credits for completion). Type of Completion: zk (examination).
Teacher(s)
Mgr. Josef Houser, Ph.D. (lecturer)
Mgr. Filip Melicher (lecturer)
MVDr. Eva Paulenová, Ph.D. (lecturer)
prof. RNDr. Michaela Wimmerová, Ph.D. (lecturer)
Guaranteed by
prof. RNDr. Michaela Wimmerová, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Timetable
Thu 15:00–15:50 C04/118
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 aim of the course is to introduce students to the problem of structural motives of proteins and nucleic acids, to methods for 3D protein structure determination, to physical-chemical principles of protein interactions and application of this knowledge for design of biologically active molecules.
Learning outcomes
On successful completion of the course, a learner will be able to: describe basic structural motives in proteins and nucleic acids; describe theoretical principles of methods for 3D structure prediction of proteins; interpret relationship between 3D structure and biological function; illustrate practical applicability of the principles for design of biologically active molecules.
Syllabus
  • 1. Introduction, definition of field, content of subject, relation to other scientific disciplines 2. Protein structure, structure of nucleic acids, structural motifs 3. Membrane proteins, signal sequence, transmembrane regions, topology 4. Structure of saccharides, oligo- and polysaccharides, saccharide sequence code, 3D structure, structure of lipids 5. Experimental techniques for structure determination, diffraction techniques, NMR, electron microscopy 6. Structural data, raw data, processed data, formats, PDB, CIF, structural databases 7. Validation of structural data, data quality, R-factor, B-factor, Ramachandran diagram 8. Prediction of protein structure, ab initio modelling, homology modelling, threading 9. Protein-small molecule interaction, molecular docking 10. Protein-macromolecule interaction, interactome 11. Protein engineering, design of mutations, protein stability 12. Drug design, in silico screening
Literature
  • Structural bioinformatics. Edited by Philip E. Bourne - Helge Weissig. Hoboken, N.J.: Wiley-Liss, 2003, xix, 649. ISBN 0471201995. info
Teaching methods
Theoretical lecture.
Assessment methods
Oral examination. The course is possible to fulfil as colloquium.
Language of instruction
Czech
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 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2014, Autumn 2015, Autumn 2016, autumn 2017, Autumn 2018, Autumn 2019, Autumn 2020, Autumn 2022, Autumn 2023, Autumn 2024.
  • Enrolment Statistics (autumn 2021, recent)
  • Permalink: https://is.muni.cz/course/sci/autumn2021/C3210