Journal
CONCEPTS IN MAGNETIC RESONANCE PART A
Volume 20A, Issue 1, Pages 24-41Publisher
WILEY-HINDAWI
DOI: 10.1002/cmr.a.10094
Keywords
ligand-protein binding; pulsed-field gradients; NMR spectroscopy; diffusion measurements
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available