Synopsis
NMR spectroscopy developed very rapidly during the past decades. Modern NMR spectroscopy is widely used in the structural biology. As one of the major methods for macromolecule structure determination at the atomic level, NMR is unique in its ability of determining the macromolecule structure in aqueous solution close to the physiological condition. The ability of detecting molecular motions of macromolecules on a large range of time scales makes NMR spectroscopy an ideal tool suitable not only for structure determination but also for molecular dynamics studies.
This short entry aims to briefly introduce the general process of solving a protein structure using NMR spectroscopy. Instead of emphasizing on the theory, the effort was put into an introduction of...
References
Brunger AT (2007) Version 1.2 of the crystallography and NMR system. Nat Protoc 2:2728–2733
Clore GM, Gronenborn AM, Bax A (1998) A robust method for determining the magnitude of the fully asymmetric alignment tensor of oriented macromolecules in the absence of structural information. J Magn Reson 133:216–221
Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289–302
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293
Fernandez C, Wider G (2003) TROSY in NMR studies of the structure and function of large biological macromolecules. Curr Opin Struct Biol 13:570–580
Fiaux J, Bertelsen EB, Horwich AL, Wuthrich K (2004) Uniform and residue-specific 15N-labeling of proteins on a highly deuterated background. J Biomol NMR 29:289–297
Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:283–291
Lipsitz RS, Tjandra N (2004) Residual dipolar couplings in NMR structure analysis. Annu Rev Biophys Biomol Struct 33:387–413
Pervushin K, Riek R, Wider G, Wuthrich K (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci U S A 94:12366–12371
Tugarinov V, Kay LE (2003) Ile, Leu, and Val methyl assignments of the 723-residue malate synthase G using a new labeling strategy and novel NMR methods. J Am Chem Soc 125:13868–13878
Zhu G, Xia Y, Lin D, Gao X (2004) TROSY-based correlation and NOE spectroscopy for NMR structural studies of large proteins. Methods Mol Biol 278:57–78
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Hu, Q. (2014). NMR Approaches to Determine Protein Structure. In: Bell, E. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6436-5_32-2
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DOI: https://doi.org/10.1007/978-1-4614-6436-5_32-2
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Publisher Name: Springer, New York, NY
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