@article {268,
	title = {Optical detection of NMR J-spectra at zero magnetic field},
	journal = {Journal of Magnetic Resonance},
	volume = {199},
	year = {2009},
	note = {J Magn Reson456YJTimes Cited:19Cited References Count:26},
	month = {Jul},
	pages = {25-29},
	abstract = {<p>Scalar couplings of the form JI(1) . I(2) between nuclei impart valuable information about molecular structure to nuclear magnetic-resonance spectra. Here we demonstrate direct detection of J-spectra due to both heteronuclear and homonuclear J-coupling in a zero-field environment where the Zeeman interaction is completely absent. We show that characteristic functional groups exhibit distinct spectra with straightforward interpretation for chemical identification. Detection is performed with a microfabricated optical atomic magnetometer, providing high sensitivity to samples of microliter volumes. We obtain 0.1 Hz linewidths and measure scalar-coupling parameters with 4-mHz statistical uncertainty. We anticipate that the technique described here will provide a new modality for high-precision\&quot; J spectroscopy\&quot; using small samples oil microchip devices for multiplexed Screening, assaying, and sample identification in chemistry and biomedicine. (C) 2009 Elsevier Inc. All rights reserved.</p>
},
	keywords = {cells},
	isbn = {1090-7807},
	doi = {Doi 10.1016/J.Jmr.2009.03.008},
	url = {<Go to ISI>://WOS:000266890300004},
	author = {Ledbetter, M. P. and Crawford, C. W. and Pines, A. and Wemmer, D. E. and Knappe, S. and Kitching, J. and Budker, D.}
}
@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 {558,
	title = {Observation of Molecular-Reorientation in Ice by Proton and Deuterium Magnetic-Resonance},
	journal = {Journal of the American Chemical Society},
	volume = {110},
	year = {1988},
	note = {J Am Chem SocP7649Times Cited:80Cited References Count:16},
	month = {Aug 17},
	pages = {5668-5671},
	isbn = {0002-7863},
	doi = {Doi 10.1021/Ja00225a013},
	url = {<Go to ISI>://WOS:A1988P764900013},
	author = {Wittebort, R. J. and Usha, M. G. and Ruben, D. J. and Wemmer, D. E. and Pines, A.}
}
