Mark P. Foster

Foster.281@osu.edu
Office: 734 Riffe Bldg.
Ph: 2-1377, LAB: 688-8146

Useful References:

Cavanagh, et al., Protein NMR, Academic Press, 1996
Evans, Biomolecular NMR Spectroscopy, Oxford University Press, 1995 (revised 1996)
Derome, Modern NMR Techniques for Chemistry Research, Pergamon Press, 1987
Grant and Harris, Eds., Encyclopedia of Nuclear Magnetic Resonance, Wiley, 1996
Jardetsky and Roberts, NMR in Molecular Biology, Academic Press, 1981
Wütrich, NMR of Proteins and Nucleic Acids, Wiley, 1986
Methods in Enzymology, v. 239, 261, 317, 338-339

Journal of Magnetic Resonance (J. Magn. Reson.)
Journal of Biomolecular NMR (J. Biomol. NMR)
Progress in NMR Spectrocopy
Journal of the American Chemical Society (J. Am. Chem. Soc.)

1. Nuclear spin, precession, spin states, equilibrium magnetization, CW NMR, FT NMR, vector model, rotating frame, radio frequency pulses, chemical shift.
2. Scalar coupling, magnetization/polarization transfer, relaxation, NOE, dynamics (fast, intermediate and slow exchange).
3. The NMR spectrometer.

1. Proteins: amino acids, chemical shifts, spin systems, secondary structures, NOEs, coupling constants.
2. Nucleic acids: nucleotides, chemical shifts, spin systems, structures, base pairing.
3. Obtaining resonance assignments: nD NMR.

1. Structure determination: Distance geometry, restrained molecular dynamics simulations (simulated annealing).
2. Molecular recognition, chemical shift mapping, filtered experiments, SAR by NMR, transfer NOE, drug design, complexes.

Basics of NMR http://www.cis.rit.edu/htbooks/nmr
NMR Knowledge Base http://www.nmr.de/
BioMagResBank http://www.bmrb.wisc.edu/