C7995 Advanced Methods of Biomolecular NMR

Faculty of Science
Autumn 2014
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 offered to students of any study field.
Course objectives
At the end of the course students should have hands-on knowledge of sophisticated experiments used in modern NMR spectroscopy with an accent on techniques for spectroscopy of proteins and nucleic acids. All important experimental issues from sample preparation and spectrometer setup and calibration trough data acquisition 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
Study Materials
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
The course is also listed under the following terms Autumn 2007 - for the purpose of the accreditation, Autumn 2010 - only for the accreditation, Autumn 2002, Autumn 2003, Autumn 2004, Autumn 2005, Autumn 2006, Autumn 2007, Autumn 2008, Autumn 2009, Autumn 2010, Autumn 2011, Autumn 2011 - acreditation, Autumn 2012, Autumn 2013, Autumn 2015, Spring 2016, Autumn 2016, Spring 2017, autumn 2017, spring 2018, Autumn 2018, Spring 2019, Autumn 2019, Spring 2020, Autumn 2020, Spring 2021, autumn 2021, Spring 2022, Autumn 2022, Spring 2023, Autumn 2023, Spring 2024, Autumn 2024, Spring 2025.
  • Enrolment Statistics (Autumn 2014, recent)
  • Permalink: https://is.muni.cz/course/sci/autumn2014/C7995