PřF:C9530 Structural biochemistry - Course Information
C9530 Structural biochemistry
Faculty of ScienceAutumn 2001
- Extent and Intensity
- 2/0. 3 credit(s). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer)
prof. RNDr. Břetislav Brzobohatý, CSc. (lecturer)
prof. Mgr. Jiří Damborský, Dr. (lecturer)
Mgr. Eva Fadrná, Ph.D. (lecturer) - Guaranteed by
- prof. Mgr. Lukáš Žídek, Ph.D.
- Prerequisites
- The course is offered to students of biochemistry and related areas (molecular biology, biophysics) and to all who are interested in modern methods of structure determination of biomacromolecules.
- 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 23 fields of study the course is directly associated with, display
- Course objectives
- The aim of the course is to offer basic information about structure determination of biomacromolecules (especially proteins and nucleic acids). The course is designed as a general overview offered to students who do not plan to enter this research area, but it may serve as an introduction to advanced courses of structure analysis. An introductory overview of basic structural motifs will be followed by discussion of methods of determination of 3D structure of macromolecules. The course will be focused on two fundamental techniques - X-ray crystallography and NMR spectroscopy. Methods of molecular mechanics and dynamics used in structure calculations based on experimental data will be described. Techniques of molecular biology utilized in protein structure determination will be discussed. Use of structure databases will be mentioned. Lectures will be presented by experts active in the discussed research areas.
- Syllabus
- 1. Structure of macromolecules, basic structural motifs of proteins and nucleic acids, structure of saccharides and membranes. 2. General characterization of proteins, methods of optical and mass spectroscopy, protein sequencing. 3. Nucleic acid sequencing, techniques of gene engineering, expression of recombinant proteins. 4-6. X-ray crystallography. Crystal preparation, diffraction experiment, methods of solving phase problem, electron density maps, structure model building. 7-9. Nuclear magnetic resonance. Isotope labeling, NMR experiment, spectral frequency assignment, determination of geometry (NOE, coupling constants), protein dynamics. 10-11. Molecular mechanics and dynamics, simulated annealing, experimental restraints. 12. Databases of structures, bioinformatics, computer prediction and modeling.
- Language of instruction
- Czech
- Further Comments
- The course is taught annually.
The course is taught: every week. - Listed among pre-requisites of other courses
- Teacher's information
- http://www.ncbr.chemi.muni.cz/~lzidek/C9530.html
- Enrolment Statistics (Autumn 2001, recent)
- Permalink: https://is.muni.cz/course/sci/autumn2001/C9530