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Solution NMR methods for quantitative identification of chemical exchange in 15 N‐labeled proteins
Author(s) -
Wang Chunyu,
Palmer Arthur G.
Publication year - 2003
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1262
Subject(s) - chemistry , triosephosphate isomerase , microsecond , relaxation (psychology) , nuclear magnetic resonance spectroscopy , hydrogen–deuterium exchange , protein dynamics , transverse relaxation optimized spectroscopy , millisecond , chemical shift , ligand (biochemistry) , allosteric regulation , nuclear magnetic resonance , computational chemistry , fluorine 19 nmr , molecular dynamics , stereochemistry , chromatography , mass spectrometry , biochemistry , psychology , social psychology , physics , astronomy , gene , receptor , enzyme
Abstract Chemical exchange phenomena in NMR spectra reveal protein motions on microsecond to millisecond time scales that are associated with biological functions, including catalysis, ligand binding, allosteric conformational changes and protein folding. This review surveys solution NMR methods for identifying chemical exchange in proteins by measuring transverse relaxation rate constants for backbone 15 N spins. The relaxation‐compensated‐ I z S z and in‐phase Hahn echo methods are suitable for small‐ to medium‐sized proteins. The transverse relaxation optimized spectroscopy method is suitable for large, deuterated proteins. Differential multiple quantum relaxation is also a signature of chemical exchange and provides unique information about exchange processes. The various methods are illustrated by application to basic pancreatic trypsin inhibitor and triosephosphate isomerase. Copyright © 2003 John Wiley & Sons, Ltd.