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