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Review
. 2011 Apr;18(4):373-9.
doi: 10.2174/092986611794653897.

Probing protein dynamics by nuclear magnetic resonance

Kong Hung Sze  1 , Pok Man Lai
Affiliations
Review

Probing protein dynamics by nuclear magnetic resonance

Kong Hung Sze et al. Protein Pept Lett. 2011 Apr.

Abstract

Proteins are dynamic molecules that often undergo conformational changes while performing their specific functions, such as target recognition, ligand binding and catalysis. NMR spectroscopy is uniquely suited to study protein dynamics, because site-specific information can be obtained for motions that span a broad range of time scales. The information obtained from NMR dynamics experiments has provided insights into specific structural changes or conformational energetics associated with molecular function. In the last decade, a number of new advancements in NMR methodologies have further extended our ability to characterize protein dynamics. Here, we present an overview of current NMR technology that is used to monitor the dynamic properties of proteins.

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