C6770 NMR Spectroscopy of Biomolecules

Faculty of Science
spring 2018
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)
doc. RNDr. Radovan Fiala, CSc. (lecturer)
Konstantinos Tripsianes, Ph.D. (lecturer)
Guaranteed by
prof. Mgr. Lukáš Žídek, Ph.D.
National Centre for Biomolecular Research – Faculty of Science
Contact Person: prof. Mgr. Lukáš Žídek, Ph.D.
Supplier department: National Centre for Biomolecular Research – Faculty of Science
Timetable
Tue 9:00–10:50 C04/211
Prerequisites
C5320 Theoretical Concepts of NMR
The course is offered to students interested in NMR methods applied to biomacromolecules. Basic knowledge of structure of proteins and nucleic acids is expected.
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 course will provide introduction to modern NMR techniques which can be applied to extract structural information for small and mid-size biological macromolecules - peptides, proteins, DNA and RNA oligonucleotides. Experimental procedures and computational protocols for determination of three-dimensional structures and dynamics based on NMR data will be discussed. Students who finish the course successfully will understand principles of NMR and its applications to biochemical problems described in original research articles, to analyze NMR experiments and design their modification, to chose the correct approach of solving a given problem, and to combine results of individual approaches to obtain a complex picture of the studied problem. The course is designed so that students who continue to study in a PhD program will be able to apply the learned skills in their own research projects.
Syllabus
  • 1. NMR as a tool for structure biology
  • 2. Basic NMR experiments, spin alchemy in heteronuclear systems
  • 3. NMR of proteins: basic ideas
  • 4. NMR of proteins: technical issues
  • 5. Homonuclear systems, equivalent nuclei, strong coupling
  • 6. TOCSY
  • 7. NMR of nucleic acids I (R. Fiala)
  • 8. NMR of nucleic acids II (R. Fiala)
  • 9. Practical application of protein NMR spectroscopy I (K. Tripsianes)
  • 10. Practical application of protein NMR spectroscopy II (K. Tripsianes)
  • 11. NMR relaxation and dynamics of molecules I
  • 12. NMR relaxation and dynamics of molecules II
  • 13. Interactions, exchange
Literature
  • CAVANAGH, John. Protein NMR spectroscopy : principles and practice. 2nd ed. Amsterdam: Elsevier, 2007, xxv, 885. ISBN 9780121644918. info
Teaching methods
Lectures combining explanation of basic ideas with analysis of model examples, computer simulations of the discussed topics.
Assessment methods
Oral examination in a form of discussion of problems solved by the student.
Language of instruction
English
Follow-Up Courses
Further Comments
Study Materials
The course is taught annually.
Teacher's information
http://www.ncbr.chemi.muni.cz/~lzidek/C6770/C6770.html
The course is also listed under the following terms Spring 2008 - for the purpose of the accreditation, Spring 2011 - only for the accreditation, Spring 2000, Spring 2001, Spring 2002, Spring 2003, Spring 2004, Spring 2005, Spring 2006, Spring 2007, Spring 2008, Spring 2009, Spring 2010, Spring 2011, Spring 2012, spring 2012 - acreditation, Spring 2013, Spring 2014, Spring 2015, Spring 2016, Spring 2017, Spring 2019, Autumn 2019, Autumn 2020, autumn 2021, Autumn 2022, Autumn 2023, Autumn 2024.
  • Enrolment Statistics (spring 2018, recent)
  • Permalink: https://is.muni.cz/course/sci/spring2018/C6770