Last updated November, 2003
Recommended Library Books at the Harman Library,
- Protein NMR Spectroscopy; Principles and Practice, J. Cavanagh, W. J. Fairbrother, A. G. Palmer III, N. J. Skelton
- NMR of Proteins and Nucleic Acids, K. WŁthrich
- Methods in enzymology. Nuclear magnetic resonance of biological macromolecules A, T. L. James
- Methods in enzymology. Nuclear magnetic resonance of biological macromolecules B, T. L. James
Nucleic Acid NMR:
Particularly Useful References: (Partial list for reference only, Not necessarily first publication in field!!!!)
NMR Pulse Sequence References:
TOCSY:Bax, A. & Davis, D.G. (1985) MLEV-17 based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
A., Ernst, R.R. & WŁthrich, K. (1980) A two-dimensional nuclear Overhauser
enhancement (2D NOE) experiment for the elucidation of complete proton-proton
cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res.
Commun. 95, 1-6.
Macura, S. & Ernst, R.R. (1980) Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41, 95-117.
COSY45: 2D homonuclear shift correlation using 45 degree read pulse W.P. Aue, E. Bartholdi, R.R. Ernst, J. Chem. Phys. 64, 2229 (1976) K. Nagayama et al., J. Magn. Reson. 40, 321 (1980)
HMQC: A. Bax, R.H. Griffey & B.L. Hawkins, J. Magn. Reson. 55, 301-315 (1983) Correlation Of Proton And N-15 Chemical-Shifts By Multiple Quantum NMR
HSQC: A.G. Palmer III, J. Cavanagh, P.E. Wright and M. Rance, J. Magn. Reson. 93, 151-170, (1991). Sensitivity improvement in proton detected heteronuclear correlation experiments; Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114: 10663- 10665.
COSY DQF Phase sensitive: 2D homonuclear shift correlation phase sensitive using TPPI with double quantum filter phasecycle: A. Derome & M. Williamson, J. Magn. Reson. 88, 177 - 185 (1990)
NOESY gradients: 2D homonuclear correlation via dipolar coupling dipolar coupling may be due to noe or chemical exchange. phase sensitive using States-TPPI method with gradient pulses in mixing time, J. Jeener, B.H. Meier, P. Bachmann & R.R. Ernst, J. Chem. Phys. 71, 4546-4553 (1979) R. Wagner & S. Berger, J. Magn. Reson. 123 A, 229-232 (1996); 2D homonuclear correlation via dipolar coupling dipolar coupling may be due to noe or chemical exchange. M. Piotto, V. Saudek & V. Sklenar, J. Biomol. NMR 2, 661 - 666 (1992); V. Sklenar, M. Piotto, R. Leppik & V. Saudek, J. Magn. Reson., Series A 102, 241 -245 (1993)
ROESY: 2D ROESY with cw spinlock for mixing phase sensitive using States-TPPI method, A. Bax & D.G. Davis, J. Magn. Reson 63, 207-213 (1985)
ROESY gradients: 2D ROESY with cw spinlock for mixing phase sensitive using States-TPPI
method water suppression using
HMBC: A. Bax and M.F. Summers: 1H and 13C assignments from sensitivity enhanced detection of heteronuclear multiple-bond connectivity by two-dimensional multiple quantum NMR. J. Am. Chem. Soc. 108, 2093-2094 (1986).
WATERGATE WATER SUPRESSION: Piotto, M., Saudek, V. and Sklenar, V.; J. Biomol. NMR 1992, 2, 661: Gradient-tailored Excitation for Single-quantum NMR Spectroscopy of Aqueous Solutions.
WŁthrich Methodology: WŁthrich, K. (1986) NMR of Proteins and Nucleic Acids, John Wiley & Sons,
. New York
Temperature dependence: Dyson HJ, Rance M, Houghten RA, Lerner RA,
. Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn. J Mol Biol. 1988 May 5;201(1):161-200. Wright PE
Deviations from aH chemical shift: Wishart, D.S., Sykes, B.D. and Richards, F.M (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651.
References to Programs:
XPLOR: Nilges, M.,
Kuszewski, J. & Brunger, A.T. (1991) Sampling properties of simulated
annealing and distance geometry. In Computational Aspects of the Study of
Biological Macromolecules by NMR (Hoch, J.C., ed.) pp 451-455, Plenum Press,
MOLMOL: "Figure prepared with the program MOLMOL (Koradi et al., 1996)": Koradi, R., Billeter, M., and W?thich, K. (1996) J Mol Graphics 14, 51-55. MOLMOL: a program for display and analysis of macromolecular structures.
DelPhi: Honig, B., Sharp, K. & Yang, A.-S. (1993) Macroscopic Models of Aqueous Solutions: Biological and Chemical Applications. J. Phys. Chem. 97, 1101-1109.
GRASP: Anthony Nicholls, Kim Sharp and Barry Honig, PROTEINS, Structure, Function and Genetics, Vol. 11, No.4, 1991, pg. 281ff
MARDIGRAS: B.A. Borgias and T.L. James, J. Magn. Reson., 87, 475-487 (1990); B.A. Borgias and T.L. James, Meth. Enzymol., 176 (1989); B.A. Borgias, M. Gochin, D.J. Kerwood, and T.L. James, In Progress in Nuclear Magnetic Resonance Spectroscopy, J.W. Emsley, J. Feeney, L.H. Sutcliffe (Eds), Oxford: Pergamon Press, 22, 83-100 (1990); T.L. James, Curr. Opin. Struct. Biol., 1, 1042-1053, (1991).
CORMA: J. W. Keepers and T. L. James, J. Magn. Reson. 57 404-426 (1984); B.A. Borgias and T.L. James, J. Magn. Reson. 79 493-512 (1988);
AMBER: Pearlmen, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham, III, T.E., DeBolt, S., Ferguson, D., Seibel G. & Kollman, P. (1995) AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comp. Phys. Commun. 91, 1-41.
XPLO2D: Kleywegt, G.J. & Jones, T.A. (1997) Model-building and refinement practice. Methods Enzymol. 277, 208-230.
PROCHECK: Laskowski, R.A., Rullmann, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.
Last updated November, 2003