@article {1515,
	title = {Termolecular kinetics for the Mu+CO+M recombination reaction: A unique test of quantum rate theory},
	journal = {Journal of Chemical Physics},
	volume = {125},
	number = {1},
	year = {2006},
	note = {ISI Document Delivery No.: 061CTTimes Cited: 0Cited Reference Count: 66Pan, James J. Arseneau, Donald J. Senba, Masayoshi Garner, David M. Fleming, Donald G. Xie, Tiao Bowman, Joel M.},
	month = {Jul},
	pages = {13},
	type = {Article},
	abstract = {The room-temperature termolecular rate constants, k(0), for the Mu+CO+M reversible arrow MuCO+M (M=He, N-2, Ar) recombination reaction have been measured by the mu SR technique, and are reported for moderator gas pressures of up to similar to 200 bar (densities less than or similar to 0.4x10(22) molec cm(-3)). The experimental relaxation rates reveal an unusual signature, in being dominated by the electron spin-rotation interaction in the MuCO center dot radical that is formed in the addition step. In N-2 moderator, k(0)=1.2 +/- 0.1x10(-34) cm(6) s(-1), only about 30\% higher than found in Ar or He. The experimental results are compared with theoretical calculations carried out on the Werner-Keller-Schinke (WKS) surface [Keller , J. Chem. Phys. 105, 4983 (1996)], within the framework of the isolated resonance model (IRM). The positions and lifetimes of resonance states are obtained by solving the complex Hamiltonian for the nonrotating MuCO system, using an L-2 method, with an absorbing potential in the asymptotic region. Accurate values of the vibrational bound and resonance states of MuCO reveal unprecedented isotope effects in comparisons with HCO, due to the remarkable effect of replacing H by the very light Mu atom (m(Mu)approximate to 1/9m(H)). Due to its pronounced zero-point energy shift, there are only two (J=0) bound states in MuCO. Contributions from nonzero J states to the termolecular rate constants are evaluated through the J-shifting approximation, with rotational constants evaluated at the potential minimum. The value of the important A constant (181 cm(-1)) used in this approximation was supported by accurate J=K=1 calculations, from which A=180 cm(-1) was obtained by numerical evaluation. The calculations presented here, with a "weak collision factor" beta(c)=0.001, indicative of the very sparse density of MuCO states, give a very good account of both the magnitude and pressure dependence of the experimental rates, but only when the fact that the two initially bound (J=0) states become resonances for J > 0 is taken into account. This is the first time in IRM calculations of atom-molecule recombination reactions where J not equal 0 states have proven to be so important, thus providing a truly unique test of quantum rate theory. (c) 2006 American Institute of Physics.},
	keywords = {ADDITION-REACTIONS, DISSOCIATION DYNAMICS, FIELD-DEPENDENCE, GAS-PHASE, RATE-CONSTANT, RESOLUTION SPECTROSCOPIC DATA, RESONANCE ENERGIES, SPIN RELAXATION, thermal, THERMODYNAMIC PROPERTIES, UNIMOLECULAR, VIBRATIONALLY EXCITED DCO((X)OVER-TILDE(2)A{\textquoteright})},
	isbn = {0021-9606},
	url = {<Go to ISI>://000238849500019},
	author = {Pan, J. J. and Arseneau, D. J. and Senba, M. and Garner, D. M. and Fleming, Donald G. and Xie, T. and Bowman, J. M.}
}
@article {818,
	title = {The crystal structure of a simple enol formed in a single-crystal-to-single-crystal enolene rearrangement},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {82},
	number = {2},
	year = {2004},
	note = {ISI Document Delivery No.: 802BHTimes Cited: 1Cited Reference Count: 15},
	month = {Feb},
	pages = {301-305},
	type = {Article},
	abstract = {When crystals of 9-tricyclo[4.4.1.0]undecalyl-4-(carbomethoxy)phenyl ketone (1) were allowed to stand in the dark for extended periods of time at room temperature, the compound underwent a thermal reaction - the enolene rearrangement - to afford enol 2. The crystals remained transparent and appeared unchanged in shape as the reaction proceeded. X-ray diffraction data were collected on single crystals containing 17\%, 25\%, 66\%, and 100\% of the enol. The crystal structure of a simple enol was obtained via this novel single-crystal-to-single-crystal enolene rearrangement.},
	keywords = {enol, enolene, HYDROGEN-ATOM ABSTRACTION, PHOTODIMERIZATION, REARRANGEMENT, single crystal, STATE, thermal},
	isbn = {0008-4042},
	url = {<Go to ISI>://000220138500026},
	author = {Chong, K. C. W. and Patrick, B. O. and Scheffer, J. R.}
}
@article {3720,
	title = {Multiple pathways for denaturation of horse plasma gelsolin},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {74},
	number = {1},
	year = {1996},
	note = {ISI Document Delivery No.: UE605Times Cited: 1Cited Reference Count: 38},
	pages = {101-107},
	type = {Article},
	abstract = {Gelsolin purified from horse plasma carries a surface charge distribution that greatly influences how the protein unfolds, aggregates, or precipitates as a function of temperature or concentration of chemical denaturant. Modification of gelsolin with fluorescein isothiocyanate replaces positive charges on amine groups with bulky, negatively charged fluorescein moieties. This postpones thermally induced precipitation by about 10 degrees C [Koepf, E.K., and Burtnick, L.D. 1993. Eur. J. Biochem. 212: 713-718]. Interaction with cations such as Ca2+ or guanidinium(+) also alters the surface charge on gelsolin. This affects the structure of the protein in solution, modifies the pathway for unfolding, and moderates the onset of precipitation induced by chemical denaturants or heat. Denaturation of gelsolin is not interpretable in terms of a simple two-state cooperative mechanism. The pathway to a denatured state and intermediate structures present along the way depend upon the agent used to unfold the protein.},
	keywords = {ACTIN-BINDING-SITES, calcium, chemical, circular dichroism, denaturation, FLUORESCEIN ISOTHIOCYANATE, gelsolin, PROTEIN, thermal},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1996UE60500011},
	author = {Koepf, E. K. and Burtnick, L. D.}
}
@article {3120,
	title = {DISCRETE VELOCITY MODEL FOR AN ESCAPING SINGLE-COMPONENT ATMOSPHERE},
	journal = {Planetary and Space Science},
	volume = {42},
	number = {5},
	year = {1994},
	note = {ISI Document Delivery No.: PF109Times Cited: 3Cited Reference Count: 42},
	month = {May},
	pages = {409-419},
	type = {Article},
	abstract = {The structure of an escaping single-component planetary atmosphere is computed by direct numerical integration the nonlinear Boltzmann equation. The transition from collision-dominated behavior deep in the atmosphere to nearly collisionless behavior at great altitudes is therefore treated self-consistently for the first time. We consider a hypothetical planet having the same mass and radius as the Earth, surrounded by an atmosphere of atoms having the same mass and total hard-sphere collision cross-section as atomic hydrogen. The atmosphere is initially hydrostatic and isothermal, at a temperature of 1000 K. As the computation progresses, the atmosphere gradually escapes. Eventually, a quasi-steady state is reached in which the density decreases significantly more rapidly than the initial barometric distribution, and the temperature decreases nearly 200 K between the planetary surface and an altitude of 10,000 km. The bulk upward flow speed increases with altitude above the exobase. However, because the most energetic particles escape and are not replenished, the atmosphere gradually cools, and the deep, collision-dominated portion of the atmosphere settles towards the planet{\textquoteright}s surface. The high-velocity tail of the velocity distribution function is quite anisotropic over a large range of altitudes, and remains largely depleted of incoming unbound particles even well below the exobase. At the highest altitudes in our simulation, the population of escaping unbound particles is considerably enhanced by the streaming of such particles from the warmer and denser regions below. The computed escape flux is at least 30\% greater than the Jeans flux as a result of this effect. It is suggested that computations similar to this one may prove useful for studying atmospheric escape from the primeval terrestrial planets, comets and Pluto.},
	keywords = {BOLTZMANN-EQUATION, ESCAPE, GASES, HYDRODYNAMIC ESCAPE, PLANETARY ATMOSPHERE, thermal},
	isbn = {0032-0633},
	url = {<Go to ISI>://A1994PF10900006},
	author = {Merryfield, W. J. and Shizgal, B. D.}
}
@article {7358,
	title = {MONOMER AND EXCIMER FLUORESCENCE OF HORSE PLASMA GELSOLIN LABELED WITH N-(1-PYRENYL)IODOACETAMIDE},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {70},
	number = {7},
	year = {1992},
	note = {ISI Document Delivery No.: JP667Times Cited: 3Cited Reference Count: 27},
	month = {Jul},
	pages = {573-578},
	type = {Article},
	abstract = {Horse plasma gelsolin was labelled with the sulfhydryl-specific fluorescent reagent N-(1-pyrenyl)iodoacetamide. The level of incorporation of probe was 1.6 +/- 0.3 mol pyrene/mol gelsolin. The circular dichroism spectrum of pyrenyl-gelsolin and its ability to interact with muscle actin were not different from that found for unmodified gelsolin. The emission from pyrenyl-gelsolin was dominated by a broad emission band centred near 483 nm, characteristic of the presence of pyrene excimers. Analysis of excitation spectra for the monomer and excimer-type fluorescence suggested that ground-state interactions may occur between adjacent pyrenes in the gelsolin structure. In the case either of excimer formation or of ground-state pyrene-pyrene interactions in doubly labelled gelsolin molecules, the modified Cys residues must be in close proximity in the folded protein structure. Thermal denaturation of gelsolin could be monitored by observing the decrease in excimer emission that accompanied heating and unfolding of the tertiary structure. While heat treatment alone did not eliminate excimer fluorescence, digestion of gelsolin with chymotrypsin completely abolished such emission. Also, pyrenyl-gelsolin prepared and studied in 6 M guanidine-HCl exhibited fluorescence characteristic of pyrene monomers exclusively.},
	keywords = {ACTIN-FILAMENTS, BINDING, CIRCULAR-DICHROISM, denaturation, FLUORESCENCE LIFETIME, gelsolin, POLYMERIZATION, PROBE, PROTEIN, PYRENE EXCIMER FLUORESCENCE, PYRENE-ACTIN, STATE, thermal, TROPOMYOSIN},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1992JP66700008},
	author = {Silva, B. E. R. and Koepf, E. K. and Burtnick, L. D. and Turro, N. J.}
}
@article {7352,
	title = {STABILIZATION OF THE STRUCTURE OF HORSE PLASMA VITAMIN-D BINDING-PROTEIN BY DISULFIDE BONDS},
	journal = {Biochemistry and Cell Biology-Biochimie Et Biologie Cellulaire},
	volume = {70},
	number = {1},
	year = {1992},
	note = {ISI Document Delivery No.: HG742Times Cited: 1Cited Reference Count: 27},
	month = {Jan},
	pages = {10-15},
	type = {Article},
	abstract = {Vitamin D binding protein (DBP) was isolated from horse plasma in a four-step procedure that involved Affi-Gel Blue affinity chromatography, gel filtration, hydroxylapatite chromatography, and anion exchange high-pressure liquid chromatography. The yield of DBP from 80 mL of plasma was 6-7 mg. Horse plasma DBP closely resembles other plasma DBPs, being a tryptophan-free protein of M(r) 53 000. It is able to bind to and block the polymerization of monomeric actin. The secondary structure of DBP was calculated from circular dichroism measurements to be 39\% alpha-helix, 42\% beta-sheet, and 19\% random coil. Circular dichroism and fluorescence studies revealed that the disulfide bonds of DBP contribute substantial structural stabilization to the molecule with respect to thermal denaturation. The thermal stability of DBP can be used to advantage. Incorporation of a brief treatment at 70-degrees-C into the preparative scheme enables omission of one chromatographic step, without detectable alteration of the purified product.},
	keywords = {actin, circular dichroism, CIRCULAR-DICHROISM, COMPLEX, denaturation, DISULFIDE BONDS, FLUORESCENCE, GC-GLOBULIN, POLYMERIZATION, RAT, SERUM, thermal, TROPOMYOSIN, VITAMIN-D BINDING PROTEIN},
	isbn = {0829-8211},
	url = {<Go to ISI>://A1992HG74200002},
	author = {Robinson, R. C. and Burtnick, L. D.}
}
