The aim of the lecture is to introduce the theory and practice of NMR-spectroscopy of organic and biomolecules. The principles of how to evaluate complex spectra and structure elucidiation are provided. Theoretical basis of bio-NMR spectroscopy are given such as: the vector model, the product operator formalism, relaxation, nuclear Overhauser effect, polarisation transfer, scalar and dipolar coupling, population and coherence transfer, chemical shift etc.. NMR signal assignment and multidimensional NMR spectroscopy (e.g. COSY, RELAY, TOCSY, NOESY, ROESY) is introduced. Isotope labelling and spectral editing strategies (e.g. HSQC, HMBC, TOCSY-HSQC, HNCO, HNCA) are outlined. Basics of NMR structure calculation will be described, including data collection, resonance assignment, collection of structural restraints, targetfunction minimalisation and quality assessment. Different approches related to structure determination of proteins (smaller than 15 kDa, 15-30 KDa and larger than 30 kDa) are described. Comparison of NMR- and X-ray determined structures are given. Protein folding is introduced viewed by NMR specroscopy: namely thermal unfolding, hydrogen-deuterium exchange, intrinsically unstructured proteins etc.. Enzymes and their function, as seen by NMR spectroscoy. NMR spectroscopy of nucleic acids and carbohydrates will also be introduced briefly.
P.J. Hore NMR spectroscopy (Nemzeti Tankönyvkiadó, 2003)
E-Notes of the lecture Suggested literature: J.N.S.Evens Biomolecular NMR Spectrscopy (Oxford Univ. Press. 1995)
A.K.Downing Protein NMR techniques Second Ed. (Humana Press 2004)