PřF:C7995 Adv. Biomolecular NMR - Course Information
C7995 Advanced Methods of Biomolecular NMR
Faculty of ScienceAutumn 2012
- Extent and Intensity
- 2/0. 2 credit(s) (fasci plus compl plus > 4). Recommended Type of Completion: zk (examination). Other types of completion: k (colloquium).
- Teacher(s)
- doc. RNDr. Radovan Fiala, CSc. (lecturer)
prof. Mgr. Lukáš Žídek, Ph.D. (lecturer) - Guaranteed by
- doc. RNDr. Radovan Fiala, CSc.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: doc. RNDr. Radovan Fiala, CSc.
Supplier department: National Centre for Biomolecular Research – Faculty of Science - Prerequisites
- Students should have good knowledge of NMR theory at the level of the courses C5320 and/or C6770.
- 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
- Biochemistry (programme PřF, D-BCH)
- Biochemistry (programme PřF, M-CH)
- Biomolecular Chemistry (programme PřF, D-BCH)
- Chemistry (programme PřF, M-CH)
- Chemistry (programme PřF, M-CH)
- Environmental Chemistry (programme PřF, M-CH)
- Course objectives
- At the end of the course students should have hands-on knowledge of sofisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important exprimental issues from sample preparation and spectrometer setup and calibration trough data aquisition and processing up to spectra evaluation will be discussed as well as practically performed in the laboratory. At the end of the course, the students will be able to prepare independently a biomolecular sample for NMR spectroscopy, choose the appropriate experiments, set up the measurements, and process and evaluate the data.
- Syllabus
- 1. NMR sample, preparation and handling 2. Spectrometer setup 3. Spectrometer calibrations 4. Building blocks of pulse sequences 5. Programming of pulse sequences 6. Water suppression techniques 7. Homonuclear 2D experiments 8. Heteronuclear double and triple resonance experiments 9. 3D experiments for proteins and nucleic acids (HNCO, HNCa, HCCH-TOCSY, HCN) 10. Data processing 11. Analysis of protein NMR spectra 12. Analysis of NMR spectra of nucleic acids
- Literature
- NMR of macromolecules : a practical approach. Edited by Gordon C.K. Roberts. Oxford: Oxford University Press, 1993, 399 s. ISBN 0-19-963224-3. info
- CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
- BERGER, Stefan and Siegmar BRAUN. 200 and more NMR experiments : a practical course. Weinheim: Wiley-VCH, 2004, xv, 838. ISBN 3527310673. info
- CAVANAGH, John and Wayne J. FAIRBROTHER. Protein NMR Spectroscopy. Principles and Practice. San Diego: Academic Press, 1996, 587 pp. ISBN 0-12-164490-1. info
- Teaching methods
- Lectures, laboratory practice, work on a project
- Assessment methods
- Presence at the practical sessions in the NMR laboratory is required. Final examination will be based on the results of individual student projects.
- Language of instruction
- English
- Further Comments
- The course can also be completed outside the examination period.
The course is taught annually.
The course is taught: in blocks. - Teacher's information
- http://ncbr.chemi.muni.cz/~fiala/AdvancedMethods.html
- Enrolment Statistics (Autumn 2012, recent)
- Permalink: https://is.muni.cz/course/sci/autumn2012/C7995