Measuring ligand-protein binding using NMR diffusion experiments

被引:96
作者
Lucas, LH [1 ]
Larive, CK [1 ]
机构
[1] Univ Kansas, Dept Chem, Lawrence, KS 66045 USA
关键词
ligand-protein binding; pulsed-field gradients; NMR spectroscopy; diffusion measurements;
D O I
10.1002/cmr.a.10094
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Characterization of ligand-protein interactions is important because many biologically important processes are mediated by the binding of a small molecule to an enzyme or cell-surface receptor. Pulsed-field gradient nuclear magnetic resonance (PFG-NMR) spectroscopy measurements of diffusion coefficients permit noninvasive, quantitative analysis of binding over a broad range of dissociation constants and ligand:protein concentration ratios. An arsenal of specific and selective PFG-NMR methods has been developed by exploiting differential behaviors of small molecule ligands and macromolecular proteins. A discussion of several PFG-NMR methods and their relevant applications reveals the analytical value of using PFG-NMR diffusion measurements for studying ligand-protein binding, (C) 2004 Wiley Periodicals, Inc.
引用
收藏
页码:24 / 41
页数:18
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