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• W2016367377 abstract "We show that Carr-Purcell-Meiboom-Gill (CPMG) 13Calpha NMR relaxation dispersion measurements are a viable means for profiling mus-ms ligand dynamics involved in receptor binding. Critically, the dispersion is at natural 13C abundance; this matches typical pharmaceutical research settings in which ligand isotope-labeling is often impractical. The dispersion reveals ligand 13Calpha nuclei that experience mus-ms modulation of their chemical shifts due to binding. 13Calpha shifts are dominated by local torsion angles , psi, chi1; hence, these experiments identify flexible torsion angles that may assist complex formation. Since the experiments detect the ligand, they are viable even in the absence of a receptor structure. The mus-ms dynamic information gained helps establish flexibility-activity relationships. We apply these experiments to study the binding of a phospho-peptide substrate ligand to the peptidyl-prolyl isomerase Pin1." @default.
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• W2016367377 date "2008-10-04" @default.
• W2016367377 modified "2023-09-25" @default.
• W2016367377 title "Dynamics of Ligand Binding from ¹³C NMR Relaxation Dispersion at Natural Abundance" @default.
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• W2016367377 doi "https://doi.org/10.1021/ja805839y" @default.
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