C9530 Structure of biomacromolecules

Faculty of Science
Autumn 2003
Extent and Intensity
2/0/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
Teacher(s)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer)
Mgr. Eva Fadrná, Ph.D. (lecturer)
prof. RNDr. Břetislav Brzobohatý, CSc. (lecturer)
doc. RNDr. Jaromír Marek, Ph.D. (lecturer)
prof. Mgr. Jiří Damborský, Dr. (lecturer)
Guaranteed by
prof. Mgr. Lukáš Žídek, Ph.D.
Chemistry Section – Faculty of Science
Contact Person: 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
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
  • 1-3. Structure of macromolecules, basic structural motifs of proteins and nucleic acids, structure of saccharides and membranes. 4-5. Computational methods, molecular mechanics and dynamics, simulated annealing. 6. Nucleic acid sequencing, techniques of gene engineering, expression of recombinant proteins. 7. General characterization of proteins, methods of optical and mass spectroscopy, protein sequencing. 8-9. X-ray crystallography. Crystal preparation, diffraction experiment, methods of solving phase problem, electron density maps, structure model building. 10-11. Nuclear magnetic resonance. Isotope labeling, NMR experiment, spectral frequency assignment, determination of geometry (NOE, coupling constants), protein dynamics. 12. Databases of structures, bioinformatics, computer prediction and modeling.
Language of instruction
Czech
Further Comments
The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: every week.
Listed among pre-requisites of other courses
Teacher's information
http://ncbr.chemi.muni.cz/~lzidek/C9530.html
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2001, Autumn 2002, Autumn 2004, Autumn 2005, 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 2017, Autumn 2018, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023, Autumn 2024.
  • Enrolment Statistics (Autumn 2003, recent)
  • Permalink: https://is.muni.cz/course/sci/autumn2003/C9530