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• W2012316183 abstract "Flexible ligands pose challenges to standard structure-activity studies since they frequently reorganize their conformations upon protein binding and catalysis. Here, we demonstrate the utility of side chain 13C relaxation dispersion measurements to identify and quantify the conformational dynamics that drive this reorganization. The dispersion measurements probe methylene 13CH2 and methyl 13CH3 groups; the latter are highly prevalent side chain moieties in known drugs. Combining these side chain studies with existing backbone dispersion studies enables a comprehensive investigation of μs–ms conformational dynamics related to binding and catalysis. We perform these measurements at natural 13C abundance, in congruence with common pharmaceutical research settings. We illustrate these methods through a study of the interaction of a phosphopeptide ligand with the peptidyl-prolyl isomerase, Pin1. The results illuminate the side-chain moieties that undergo conformational readjustments upon complex formation. In particular, we find evidence that multiple exchange processes influence the side chain dispersion profiles. Collectively, our studies illustrate how side-chain relaxation dispersion can shed light on ligand conformational transitions required for activity, and thereby suggest strategies for its optimization." @default.
• W2012316183 created "2016-06-24" @default.
• W2012316183 creator A5022504900 @default.
• W2012316183 creator A5034464729 @default.
• W2012316183 creator A5085781283 @default.
• W2012316183 date "2009-07-29" @default.
• W2012316183 modified "2023-09-24" @default.
• W2012316183 title "Mapping the dynamics of ligand reorganization via 13CH3 and 13CH2 relaxation dispersion at natural abundance" @default.
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• W2012316183 doi "https://doi.org/10.1007/s10858-009-9349-4" @default.
• W2012316183 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2846628" @default.
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