@article {4771,
	title = {Bis-capsules: Cooperative reversible encapsulation of two molecules in adjacent separate chambers},
	journal = {Angewandte Chemie-International Edition},
	volume = {39},
	number = {1},
	year = {2000},
	note = {ISI Document Delivery No.: 273GWTimes Cited: 31Cited Reference Count: 27},
	pages = {194-+},
	type = {Article},
	keywords = {CALIXARENES, CARCEPLEXES, CAVITANDS, COMPLEXES, GUESTS, host-guest chemistry, HOSTS, HYDROGEN-BONDS, molecular recognition, NONCOVALENT INTERACTIONS, TEMPLATION},
	isbn = {1433-7851},
	url = {<Go to ISI>://000084700400026},
	author = {Chopra, N. and Naumann, C. and Sherman, J. C.}
}
@article {4006,
	title = {Dissociation of heme from myoglobin and cytochrome b(5): Comparison of behavior in solution and the gas phase},
	journal = {Biochemistry},
	volume = {36},
	number = {5},
	year = {1997},
	note = {ISI Document Delivery No.: WG072Times Cited: 79Cited Reference Count: 6144th ASMS Conference on Mass Spectrometry and Allied TopicsMAY 12-16, 1996PORTLAND, ORASMS},
	month = {Feb},
	pages = {1018-1025},
	type = {Proceedings Paper},
	abstract = {The relationship of the structure of a protein in solution to the structure of a gas-phase protein ion and the manner in which gas-phase protein ions bind small molecules noncovalently are topics of current debate. To address these issues, the stability of heme binding to wild-type and variant forms of apomyoglobin and apocytochrome bs has been studied in the gas phase by electrospray mass spectrometry (ES-MS) and compared with the stability of heme binding to the same proteins in solution. The voltage required to dissociate ions of the heme-protein complexes in the orifice-skimmer region of an electrospray mass spectrometer, a measure of the complex stability, is found to be correlated with the activation energy for dissociation of the complexes in solution across a series of proteins in which the number of hydrogen bonds between the heme propionate groups and surface residues is systematically reduced. However, variants in which the hydrogen bonds to the proximal histidine have been removed are destabilized in solution but stabilized in the gas-phase ions. These results suggest that on the millisecond time scale of the ES-MS experiment, the gas-phase protein ion may retain much of the structure of the protein in solution, at least for those residues surrounding the heme group. Furthermore, the ability of ES-MS to detect relatively subtle differences in protein-small molecule complex stability demonstrated in this work suggests that this technique may be a convenient, sensitive, and generally useful strategy for physical characterization of such complexes.},
	keywords = {ATMOSPHERIC-PRESSURE, CONFORMATION, ELECTROSPRAY MASS-SPECTROMETRY, FEATURES, IONIZATION, LARGE MOLECULES, NONCOVALENT INTERACTIONS, PROTEIN IONS, REORIENTATION, STABILITY},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1997WG07200006},
	author = {Hunter, C. L. and Mauk, A. G. and Douglas, D. J.}
}
@article {3936,
	title = {An extended mass range quadrupole for electrospray mass spectrometry},
	journal = {International Journal of Mass Spectrometry and Ion Processes},
	volume = {162},
	number = {1-3},
	year = {1997},
	note = {ISI Document Delivery No.: XD007Times Cited: 10Cited Reference Count: 39},
	month = {Mar},
	pages = {121-127},
	type = {Article},
	abstract = {The mass range of a quadrupole mass spectrometer with an electrospray source has been increased from m/z 4000 to m/z 8585 by lowering the radio frequency of the quadrupole power supply from 1.00 MHz to 683 kHz. Unit mass resolution at m/z 5030 can be achieved. The sensitivity below m/z 3000 shows only small changes as expected from phase space arguments. Spectra of poly propylene glycol and soybean agglutinin with peaks in the range m/z 4000-7000 are described. (C) 1997 Elsevier Science B.V.},
	keywords = {CLUSTERS, COMPLEXES, CONFORMATIONAL-CHANGES, DISSOCIATION, ELECTROSPRAY, high mass, IONIZATION-POTENTIALS, IONS, non-covalent, NONCOVALENT INTERACTIONS, PROTEINS, quadrupole mass spectrometer, SOYBEAN AGGLUTININ},
	isbn = {0168-1176},
	url = {<Go to ISI>://A1997XD00700011},
	author = {Collings, B. A. and Douglas, D. J.}
}
