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Small molecule conformation in the receptor‐bound state by the two‐dimensional spin exchange experiment
Author(s) -
Andersen Niels H.,
Eaton Hugh L.,
Nguyen Khe T.
Publication year - 1987
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.1260251202
Subject(s) - chemistry , two dimensional nuclear magnetic resonance spectroscopy , nuclear overhauser effect , relaxation (psychology) , spin diffusion , spin (aerodynamics) , bound state , phase (matter) , nuclear magnetic resonance , diffusion , nuclear magnetic resonance spectroscopy , analytical chemistry (journal) , molecular physics , stereochemistry , physics , quantum mechanics , thermodynamics , chromatography , psychology , social psychology , organic chemistry
Pure absorption phase two‐dimensional nuclear Overhauser spectrocopy (NOESY), using a short cycle time protocol, has been used to study cross‐relaxation between protons of ligands bound to proteins. The 2D experiment is an accurate and efficient method for determining exchange transferred NOEs. Truncated NOESY data sets (obtained in less than 3 h) for the test systems—prostaglandin F 2 α bound to albumin and NAD + bound to three different dehydrogenase enzymes—provide NOE estimates within experimental error of those obtained by the more time‐consuming one‐dimensional experiments. The 2D data matrix has within it spin‐diffusion controls and cross‐relaxation spectra useful for the subtraction of unwanted signals including spin transfer from coincidentally perturbed protein resonances and t 1 streaks and ridges.