Relaxation Dispersion Studies of Enzyme Motions

Abstract : Recent developments in spin-1/2 isotope labeling and NMR pulse sequence advances have been leveraged to investigate us - ms motions in enzyme function. These studies have identified concerted motions that occur over large regions of enzymes and often involve highly conserved amino acids. In combination with functional studies these NMR-identified motions have been implicated in partaking in the rate-determining step in the catalytic cycle. This review examines several of the more recent solution NMR studies that demonstrate the essential nature of conformational motions.
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Contributor : Nicolas Doucet <>
Submitted on : Monday, October 1, 2012 - 4:48:31 AM
Last modification on : Monday, October 8, 2018 - 5:44:05 PM

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Nicolas Doucet, J Patrick Loria. Relaxation Dispersion Studies of Enzyme Motions. Advances in Biomedical Spectroscopy., IOS Press, pp.185-202, 2011, Biomolecular NMR Spectroscopy. Volume 3, ⟨10.3233/978-1-60750-695-9-185⟩. ⟨pasteur-00736963⟩

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