@article {354, title = {Detection and characterization of xenon-binding sites in proteins by Xe-129 NMR spectroscopy}, journal = {Journal of Molecular Biology}, volume = {322}, year = {2002}, note = {J Mol Biol597PTTimes Cited:53Cited References Count:54}, month = {Sep 13}, pages = {425-440}, abstract = {

Xenon-binding sites in proteins have led to a number of applications of xenon in biochemical and structural studies. Here we further develop the utility of Xe-129 NMR in characterizing specific xenon-protein interactions. The sensitivity of the Xe-129 chemical shift to its local environment and the intense signals attainable by optical pumping make xenon a useful NMR reporter of its own interactions with proteins. A method for detecting specific xenon-binding interactions by analysis of Xe-129 chemical shift data is illustrated using the maltose binding protein (MBP) from Escherichia coli as an example. The crystal structure of MBP in the presence of 8 atm of xenon confirms the binding site determined from NMR data. Changes in the structure of the xenon-binding cavity upon the binding of maltose by the protein can account for the sensitivity of the Xe-129 chemical shift to MBP conformation. Xe-129 NMR data for xenon in solution with a number of cavity containing phage T4 lysozyme mutants show that xenon can report on cavity structure. In particular, a correlation exists between cavity size and the binding-induced Xe-129 chemical shift. Further applications of Xe-129 NMR to biochemical assays, including the screening of proteins for xenon binding for crystallography are considered. (C) 2002 Elsevier Science Ltd. All rights reserved

}, keywords = {nonpolar cavity}, isbn = {0022-2836}, doi = {Doi 10.1016/S0022-2836(02)00739-8}, url = {://WOS:000178230500014}, author = {Rubin, S. M. and Lee, S. Y. and Ruiz, E. J. and Pines, A. and Wemmer, D. E.} }