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NMR methods for the study of protein structure and dynamics.

L E Kay
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Abstract

An understanding of the role played by a protein in cellular function requires a detailed picture of its three-dimensional structure as well as an appreciation of how the structure varies as a function of time as a result of molecular dynamics. Over the past several years, multidimensional, multinuclear solution NMR spectroscopy has become a powerful technology for obtaining both structural and dynamical information on proteins and protein-ligand systems. In the present review, a number of new methodological advances are highlighted that have significantly improved the quality of NMR spectra of biomolecules and have increased the molecular weight limitations previously imposed on NMR-based structural studies of macromolecules. Applications of this technology to a number of protein systems currently studied in my laboratory are presented.

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Carbon IsotopesDeuteriumMagnetic Resonance SpectroscopyModels, ChemicalModels, MolecularNitrogen IsotopesProtein ConformationThermodynamicssrc Homology DomainsJournal ArticleResearch Support, Non-U.S. Gov'tReview

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BibTeXRIS

L E Kay. 1997. NMR methods for the study of protein structure and dynamics.. https://doi.org/10.1139/o97-023

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