@article {299,
	title = {Optimization of xenon biosensors for detection of protein interactions},
	journal = {Chembiochem},
	volume = {7},
	year = {2006},
	note = {Chembiochem003SDTimes Cited:39Cited References Count:25},
	month = {Jan},
	pages = {65-73},
	abstract = {<p>Hyperpolarized Xe-129 NMR spectroscopy can detect the presence of specific low-concentration biomolecular analytes by means of a xenon biosensor that consists of a water-soluble, targeted cryptophane-A cage that encapsulates the xenon. In this work, we use the prototypical biotinylated xenon biosensor to determine the relationship between the molecular composition of the xenon biosensor and the characteristics of protein-bound resonances. The effects of diastereomer overlap, dipole-dipole coupling, chemical-shift anisotropy, xenon exchange, and biosensor conformotional exchange on the protein-bound biosensor signal were assessed. It was found that an optimal protein-bound biosensor signal can be obtained by minimizing the number of biosensor diastereomers and using a flexible linker of appropriate length. Both the line width and sensitivity of chemical shift to protein binding of the xenon biosensor were found to be inversely proportional to linker length.</p>
},
	keywords = {complexes},
	isbn = {1439-4227},
	doi = {Doi 10.1002/Cbic.200500327},
	url = {<Go to ISI>://WOS:000234701000012},
	author = {Lowery, T. J. and Garcia, S. and Chavez, L. and Ruiz, E. J. and Wu, T. and Brotin, T. and Dutasta, J. P. and King, D. S. and Schultz, P. G. and Pines, A. and Wemmer, D. E.}
}
@article {335,
	title = {Diamagnetic clusters of paramagnetic endometallofullerenes: A solid-state MAS NMR study},
	journal = {Journal of Physical Chemistry B},
	volume = {108},
	year = {2004},
	note = {J Phys Chem B846BKTimes Cited:10Cited References Count:39},
	month = {Aug 19},
	pages = {12450-12455},
	abstract = {<p>Solid powder samples of complexes of the endometallofullerenes (EMF) La@C-82 and Y@C-82 with hexamethylphosphoramide (HMPA) were studied by magic-angle spinning (MAS) NMR. We have obtained well-resolved P-31 NMR spectra and C-13 NMR spectra for both La-EMF/HMPA and Y-EMF/HMPA and La-139 spectra for the La-EMF/HMPA. The (31)p measurements on La-EMF/HMPA and Y-EMF/HMPA have revealed considerable chemical shifts of (31)p signals relative to pure HMPA. Two-dimensional exchange P-31 experiments revealed that HMPA molecules at different sites in the EMF/HMPA complex do not change positions at a time scale of up to 1 s. Both EMF samples demonstrate a vast chemical shift range for 31p of the bound HMPA molecules. In addition, the La-EMF/HMPA exhibits the enormous spreading of the chemical shifts for La-139. The experimental results suggest that paramagnetic La@C-82 and Y@C-92 in the solid state form clusters (nanoparticles) in which the exchange coupling of the EMF takes place with quenching of the most electron spins.</p>
},
	keywords = {complexes},
	isbn = {1520-6106},
	doi = {Doi 10.1021/Jp048610z},
	url = {<Go to ISI>://WOS:000223289500027},
	author = {Koltover, V. K. and Logan, J. W. and Heise, H. and Bubnov, V. P. and Estrin, Y. I. and Kareev, I. E. and Lodygina, V. P. and Pines, A.}
}
