1. komponenta

Lecture type	Total
Lectures	20

* Load is given in academic hour (1 academic hour = 45 minutes)

Solid state NMR, CP MAS NMR techniques, quadrupolar nuclei, correlation between solid state NMR spectra and macroscopic properties, cross-relaxation and cross-correlation, modern multipulse techniques.
Computational methods for determination of chemical shifts and spin-spin couplings, molecular dynamics and solvent models, visualisation of nuclear shielding and couplings. calculation of NMR chemical shifts in proteins and nucleic acids, characterisation of NMR tensors and couplings in hydrogen bonded systems.
Structure determination of nucleic acids by using one- and multi-dimensional NMR techniques and molecular modelling, base pairs and hydrogen bonding, interactions of cations and nucleic acids, binding kinetics studies.
Interactions of small molecules and biological receptors by NMR, transferred NOE techniques, saturation transfer difference techniques (STD), diffusion editing techniques, NMR screening (SAR by NMR and others).
description of instruction methods Lectures, seminars, demonstrations, consultations
description of course/module requirements Written and/or oral exam

1. OBVEZNA LITERATURA:
   Melinda J. Duer, Introduction to Solid-State NMR Spectroscopy, Blackwell Publishers, 2004.
   James Keeler, Understanding NMR Spectroscopy, John Wiley & Sons, 2006.
   M. Kaupp, M. Buehl, and V.G. Malkin, Calculation of NMR and EPR Parameters, Theory and Applications, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, 2004.
   O. Zerbe, Ed.: BioNMR in Drug Research. Methods and Principles in Medicinal Chemistry. Wiley-VCH, Weinheim, 2003.
2. DOPUNSKA LITERATURA:
   Suvremeni opsežniji revijski članci i znanstvene monografije

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