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Access to the article is free, however registration and sign-in are required. Structure-based drug design traditionally uses static protein models as inspirations for focusing on "active" site targets. Allosteric regulation of biological macromolecules, however, is affected by both conformational and dynamic properties of the protein or protein complex and can potentially lead to more avenues for therapeutic development. We discuss the advantages of searching for molecules that conformationally trap a macromolecule in its inactive state. Although multiple methodologies exist to probe protein dynamics and ligand binding, our current discussion highlights the use of nuclear magnetic resonance spectroscopy in the drug discovery and design process.

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      Keywords:

      NSDL,NSDL_SetSpec_BEN,oai:nsdl.org:2200/20110722022702097T,Monod-Wyman-Changeux (MWC) symmetrical model of allostery,Allosteric sites,Structure-based drug design,nuclear magnetic resonance (NMR)

      Language:

      English

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      Public - Available to anyone

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      Creative Commons Attribution Non-Commercial Share Alike

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