@article {313,
	title = {Distinguishing multiple chemotaxis Y protein conformations with laser-polarized Xe-129 NMR},
	journal = {Protein Science},
	volume = {14},
	year = {2005},
	note = {Protein Sci907SSTimes Cited:23Cited References Count:27},
	month = {Apr},
	pages = {848-855},
	abstract = {<p>The chemical shift of the Xe-129 NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show that the Xe-129 shift can sense more subtle changes: magnesium binding, BeF3- activation, and peptide binding by the Escherichia coli chemotaxis Y protein. H-1-N-15 correlation spectroscopy and X-ray crystallography were used to identify two xenon-binding cavities in CheY that are primarily responsible for the shift changes. One site is near the active site, and the other is near the peptide binding site.</p>
},
	keywords = {cavity},
	isbn = {0961-8368},
	doi = {Doi 10.1110/Ps.041231005},
	url = {<Go to ISI>://WOS:000227738900002},
	author = {Lowery, T. J. and Doucleff, M. and Ruiz, E. J. and Rubin, S. M. and Pines, A. and Wemmer, D. E.}
}
@article {333,
	title = {Design of a conformation-sensitive xenon-binding cavity in the ribose-binding protein},
	journal = {Angewandte Chemie-International Edition},
	volume = {43},
	year = {2004},
	note = {Angew Chem Int Edit877MVTimes Cited:10Cited References Count:20},
	pages = {6320-6322},
	keywords = {probe},
	isbn = {1433-7851},
	doi = {Doi 10.1002/Anie.200460629},
	url = {<Go to ISI>://WOS:000225575600015},
	author = {Lowery, T. J. and Rubin, S. M. and Ruiz, E. J. and Pines, A. and Wemmer, D. E.}
}
@article {325,
	title = {Development of a functionalized xenon biosensor},
	journal = {Journal of the American Chemical Society},
	volume = {126},
	year = {2004},
	note = {J Am Chem Soc872UHTimes Cited:60Cited References Count:76},
	month = {Nov 24},
	pages = {15287-15294},
	abstract = {<p>NMR-based biosensors that utilize laser-polarized xenon offer potential advantages beyond current sensing technologies. These advantages include the capacity to simultaneously detect multiple analytes, the applicability to in vivo spectroscopy and imaging, and the possibility of \&quot;remote\&quot; amplified detection. Here, we present a detailed NMR characterization of the binding of a biotin-derivatized caged-xenon sensor to avidin. Binding of \&quot;functionalized\&quot; xenon to avidin leads to a change in the chemical shift of the encapsulated xenon in addition to a broadening of the resonance, both of which serve as NMR markers of ligand-target interaction. A control experiment in which the biotin-binding site of avidin was blocked with native biotin showed no such spectral changes, confirming that only specific binding, rather than nonspecific contact, between avidin and functionalized xenon leads to the effects on the xenon NMR spectrum. The exchange rate of xenon (between solution and cage) and the xenon spin-lattice relaxation rate were not changed significantly upon binding. We describe two methods for enhancing the signal from functionalized xenon by exploiting the laser-polarized xenon magnetization reservoir. We also show that the xenon chemical shifts are distinct for xenon encapsulated in different diastereomeric cage molecules. This demonstrates the potential for tuning the encapsulated xenon chemical shift, which is a key requirement for being able to multiplex the biosensor.</p>
},
	keywords = {drug discovery},
	isbn = {0002-7863},
	doi = {Doi 10.1021/Ja0483037},
	url = {<Go to ISI>://WOS:000225233600051},
	author = {Spence, M. M. and Ruiz, E. J. and Rubin, S. M. and Lowery, T. J. and Winssinger, N. and Schultz, P. G. and Wemmer, D. E. and Pines, A.}
}
