@article {RADCHENKO2014721,
	title = {Desferrioxamine as an appropriate chelator for 90Nb: Comparison of its complexation properties for M-Df-Octreotide (M=Nb, Fe, Ga, Zr)},
	journal = {Nuclear Medicine and Biology},
	volume = {41},
	number = {9},
	year = {2014},
	pages = {721 - 727},
	abstract = {The niobium-90 radioisotope (90Nb) holds considerable promise for use in immuno-PET, due to its decay parameters (t{\textonehalf}=14.6h, positron yield=53\%, E{\ss}+mean=0.35MeV and E{\ss}+max = 1.5MeV). In particular, 90Nb appears well suited to detect in vivo the pharmacokinetics of large targeting vectors (50{\textendash}150kDa). In order to be useful for immuno-PET chelators are required to both stabilize the radionuclide in terms of coordination chemistry and to facilitate the covalent attachment to the targeting vector. Different chelators were evaluated for this purpose in terms of radiolabelling efficiency and stability of the radiolabelled Nb(V) complex and in order to determine the most suitable candidate for conjugation to a biologically relevant targeting vector. For the purpose of studying the complexation properties the niobium radioisotope 95Nb was used as an analogue of 90Nb, by virtue of its longer half-life (35days) and lower cost (reactor-based production). Acyclic and cyclic chelators were investigated, with desferroxamine [Df: (N{\textquoteright}-{5-[acetyl(hydroxy)amino]pentyl}-N-[5-({4-[(5-aminopentyl) (hydroxy)amino]-4-oxobutanoyl} amino)pentyl]-N-hydroxysuccinamide)] emerging as the best candidate. Greater than 99\% radiolabelling was achieved at room temperature over a wide pH range. The 95Nb-Df complex is sufficiently stable for immuno-PET (<7\% degradation over 7days in vitro). As a proof-of-principle, a Df conjugate featuring a well-established targeting vector, (D)-Phe1-octreotide, was evaluated. The fast labelling kinetics of the unconjugated chelator (Df) were retained for Df-succinyl-(D)Phe1-octreotide (Df-OC), with>90\% labelling after 1h at room temperature over the pH range 5{\textendash}7. Stability studies, performed in vitro in serum at physiological temperature (37{\textdegree}C), revealed that 87{\textpm}2\% of the radiolabelled molecule remained intact after 7days. Competition studies with relevant metal ions (zirconium(IV), gallium(III) and iron(III)) have been performed with Df-OC to gain insight to the relative stability [Nb-Df]-OC complex to transmetallation. At equimolar metal ion concentrations the [Nb-Df]-OC complex showed the greatest overall stability. The favourable radiolabelling characteristics of Df-OC and its stability indicate that Df is a potentially very useful chelator for the development of radiopharmaceuticals for 90Nb-PET.},
	keywords = {Chelators, DESFERRIOXAMINE, Df-Octereotide, Positron emitter Nb, STABILITY},
	issn = {0969-8051},
	doi = {https://doi.org/10.1016/j.nucmedbio.2014.06.006},
	url = {http://www.sciencedirect.com/science/article/pii/S0969805114004387},
	author = {Valery Radchenko and Stefan Busse and Frank Roesch}
}
@article {2366,
	title = {Calorimetric studies of the interaction between the insulin-enhancing drug candidate bis(maltolato)oxovanadium(IV) (BMOV) and human serum apo-transferrin},
	journal = {Journal of Inorganic Biochemistry},
	volume = {103},
	number = {4},
	year = {2009},
	note = {ISI Document Delivery No.: 429EUTimes Cited: 8Cited Reference Count: 31Bordbar, Abdol-Khalegh Creagh, A. Louise Mohammadi, Fakhrossadat Haynes, Charles A. Orvig, Chris6th International Vanadium SymposiumJUL 17-19, 2008Lisbon, PORTUGALSp. Iss. SI},
	month = {Apr},
	pages = {643-647},
	type = {Proceedings Paper},
	abstract = {Bis(maltolato)oxovanadium(IV) (BMOV), and its ethylmaltol analog, bis(ethymaltolato)oxovanadium(IV) (BEOV), are candidate insulin-enhancing agents for the treatment of type 2 diabetes mellitus; in mid-2008, BEOV advanced to phase 11 clinical testing. The interactions of BMOV and its inorganic congener, vanadyl Sulfate (VOSO4), with human serum apo-transferrin (hTf) were investigated using differential scanning calorimetry (DSC). Addition of BMOV or VOSO4 to apo-hTf resulted in an increase in thermal stability of both the C- and N-lobes of transferrin as a result of binding to either vanadyl compound. A series of DSC thermograms of hTf Solutions containing different molar ratios of BMOV and VOSO4 were used to determine binding constants: at 25 degrees C the binding constants of BMOV to the C- and N-lobes of apo-hTf were found to be 3 (+/- 1) x 10(5) and 1.8 (+/- 0.7) x 10(5) M-1, respectively. The cot-responding values for VOSO4 were 1.7 (+/- 0.3) x 10(5) and 7 (+/- 2) x 10(4) M-1. The results show that the vanadium species initially presented as either BMOV or VOSO4 had similar affinities for human serum transferrin due to oxidation of solvated vanadyl(IV) prior to complexation to transferrin. Binding of metavanadate (VO3-) was confirmed by DSC and isothermal titration calorimetry (ITC) experiments of the interaction between sodium metavanadate (NaVO3) and hTf. (C) 2008 Elsevier Inc. All rights reserved.},
	keywords = {Apo-transferrin, BINDING, BIS(MALTOLATO)OXOVANADIUM(IV), CHEMISTRY, COMPLEXES, Insulin-enhancing, iron, MALTOL, MOLYBDENUM, NICKEL, RATS, STABILITY, VANADIUM},
	isbn = {0162-0134},
	url = {<Go to ISI>://000264904400022},
	author = {Bordbar, A. K. and Creagh, A. L. and Mohammadi, F. and Haynes, C. A. and Orvig, Chris}
}
@article {2402,
	title = {LINEAR QUADRUPOLES IN MASS SPECTROMETRY},
	journal = {Mass Spectrometry Reviews},
	volume = {28},
	number = {6},
	year = {2009},
	note = {ISI Document Delivery No.: 515CWTimes Cited: 5Cited Reference Count: 145Douglas, D. J.},
	month = {Nov-Dec},
	pages = {937-960},
	type = {Review},
	abstract = {The use of linear quadrupoles in mass spectrometry as mass filters and ion guides is reviewed. Following a tutorial review of the principles of mass filter operation, methods of mass analysis are reviewed. Discussed are extensions of quadrupole mass filters to higher masses, scanning with frequency sweeps of the quadrupole waveform, operation in higher stability regions, and operation with rectangular or other periodic waveforms. Two relatively new methods of mass analysis the use of "islands of stability" and "mass selective axial ejection" are then reviewed. The optimal electrode geometry for a quadrupole mass filter constructed with round rods is discussed. The use of collisional cooling in quadrupole ion guides is discussed along with ion guides that have axial fields. Finally, mass analysis with quadrupoles that have large distortions to the geometry and fields is discussed. An Appendix gives a brief tutorial review of definitions of electrical potentials and fields, as well as the units used in this article. (C) 2009 Wiley Periodicals, Inc., Mass Spec Rev 28:937-960, 2009},
	keywords = {2ND STABILITY REGION, axial fields, AXIAL-FIELD, CHARGED-PARTICLE, COLLISION-INDUCED DISSOCIATION, distorted fields, FRINGING FIELDS, ion guide, ION OPTICAL-PROPERTIES, linear, mass filter, mass scans, multipoles, OCTOPOLE FIELDS, QUADRUPOLE, quadrupole excitation, RADIO-FREQUENCY, RESOLUTION, SEPARATION MODE, STABILITY, TRAJECTORIES, VOLTAGE COMPONENT},
	isbn = {0277-7037},
	url = {<Go to ISI>://000271445200005},
	author = {Douglas, D. J.}
}
@article {2309,
	title = {Conformations of Gas-Phase Ions of Ubiquitin, Cytochrome c, Apomyoglobin, and beta-Lactoglobulin Produced from Two Different Solution Conformations},
	journal = {Journal of the American Society for Mass Spectrometry},
	volume = {19},
	number = {12},
	year = {2008},
	note = {ISI Document Delivery No.: 385IWTimes Cited: 2Cited Reference Count: 36Wright, P. John Zhang, Jianmin Douglas, D. J.},
	month = {Dec},
	pages = {1906-1913},
	type = {Article},
	abstract = {At low pH in solutions of 50\% methanol, proteins form expanded denatured states (the "H" state). In 90\% methanol, proteins form expanded helical denatured states with artificial alpha-helices (the "H-c" state). Gas-phase ions of ubiquitin, cytochrome c, apomyoglobin, and native and disulfide-reduced beta-lactoglobulin were formed by electrospray ionization (EST) of the proteins from the H and H-c states in solution. Both states in solution produce the same charge states in EST. The conformations of the ions were studied with cross section measurements and gas-phase H/D exchange experiments. The cross sections show that the ions retain considerable folded structure. For a given protein and given charge state, ions produced from the H and H-c states showed the same cross sections (within similar to 1\%). Ions of cytochrome c, apomyoglobin, and native and reduced beta-lactoglobulin of a given charge state showed no differences in H/D exchange level when produced from the H or H-c state. However, ubiquitin ions produced from the H-c state consistently exchange fewer (similar to 13\%) hydrogens than ions produced from the H state, suggesting that in this case the gas-phase protein ions retain some memory of their solution conformations. (J Am Soc Mass Spectrom 2008, 19, 1906-1913) (c) 2008 Published by Elsevier Inc. on behalf of American Society for Mass Spectrometry},
	keywords = {CIRCULAR-DICHROISM, COLLISION CROSS-SECTIONS, H/D EXCHANGE, HYDROGEN/DEUTERIUM EXCHANGE, IONIZATION MASS-SPECTROMETRY, MYOGLOBIN, OF-FLIGHT, PROTEIN IONS, STABILITY, SYSTEM, TRAP},
	isbn = {1044-0305},
	url = {<Go to ISI>://000261808900023},
	author = {Wright, P. J. and Zhang, J. M. and Douglas, D. J.}
}
@article {2033,
	title = {Engineered elastomeric proteins with dual elasticity can be controlled by a molecular regulator},
	journal = {Nature Nanotechnology},
	volume = {3},
	number = {8},
	year = {2008},
	note = {ISI Document Delivery No.: 335WZTimes Cited: 12Cited Reference Count: 29Cao, Yi Li, Hongbin},
	month = {Aug},
	pages = {512-516},
	type = {Article},
	abstract = {Elastomeric proteins are molecular springs that confer excellent mechanical properties(1-5) to many biological tissues and biomaterials. Depending on the role performed by the tissue or biomaterial, elastomeric proteins can behave as molecular springs(1,2,6,7) or shock absorbers(3-5,8-10). Here we combine single-molecule atomic force microscopy and protein engineering techniques to create elastomeric proteins that can switch between two distinct types of mechanical behaviour in response to the binding of a molecular regulator. The proteins are mechanically labile by design and behave as entropic springs with an elasticity that is governed by their configurational entropy. However, when a molecular regulator binds to the protein, it switches into a mechanically stable state and can act as a shock absorber. These engineered proteins effectively mimic and combine the two extreme forms of elastic behaviour found in natural elastomeric proteins, and thus represent a new type of smart nanomaterial that will find potential applications in nanomechanics and material sciences.},
	keywords = {BINDING, BIOLOGICAL ROLES, DESIGN, DOMAINS, FORCE-SPECTROSCOPY, MECHANICAL-PROPERTIES, STABILITY, TITINS, TOPOLOGY},
	isbn = {1748-3387},
	url = {<Go to ISI>://000258325800018},
	author = {Cao, Y. and Li, H. B.}
}
@article {2287,
	title = {Toward [F-18]-labeled aryltrifluoroborate radiotracers: In vivo positron emission tomography imaging of stable aryltrifluoroborate clearance in mice},
	journal = {Journal of the American Chemical Society},
	volume = {130},
	number = {36},
	year = {2008},
	note = {ISI Document Delivery No.: 344TPTimes Cited: 15Cited Reference Count: 35Ting, Richard Harwig, Curtis auf dem Keller, Ulrich McCormick, Siobhan Austin, Pamela Overall, Christopher M. Adam, Michael J. Ruth, Thomas J. Perrin, David M.},
	month = {Sep},
	pages = {12045-12055},
	type = {Article},
	abstract = {The use of a boronic ester as a captor of aqueous [F-18]-fluoride has been previously suggested as a means of labeling biomolecules in one step for positron emission tomography (PET) imaging. For this approach to be seriously considered, the [F-18]-labeled trifluoroborate should be humorally stable such that it neither leaches free [F-18]-fluoride to the bone nor accumulates therein. Herein, we have synthesized a biotinylated boronic ester that is converted to the corresponding trifluoroborate salt in the presence of aqueous [F-18]-fluoride. In keeping with its in vitro aqueous kinetic stability at pH 7.5, the trifluoroborate appears to clear in vivo quite rapidly to the bladder as the stable trifluoroborate salt with no detectable leaching of free [F-18]-fluoride to the bone. When this labeled biotin is preincubated with avidin, the pharmacokinetic clearance of the resulting complex is visibly altered. This work validates initial claims that boronic esters are potentially useful as readily labeled precursors to [F-18]-PET reagents.},
	keywords = {apoptosis, BIODISTRIBUTION, CANCER, DESIGN, F-18, MICROPET, NO-CARRIER, PEPTIDES, PET, STABILITY},
	isbn = {0002-7863},
	url = {<Go to ISI>://000258950500044},
	author = {Ting, R. and Harwig, C. and auf dem Keller, U. and McCormick, S. and Austin, P. and Overall, C. M. and Adam,Michael J. and Ruth, T. J. and Perrin,David M.}
}
@article {2287,
	title = {Toward [F-18]-labeled aryltrifluoroborate radiotracers: In vivo positron emission tomography imaging of stable aryltrifluoroborate clearance in mice},
	journal = {Journal of the American Chemical Society},
	volume = {130},
	number = {36},
	year = {2008},
	note = {ISI Document Delivery No.: 344TPTimes Cited: 15Cited Reference Count: 35Ting, Richard Harwig, Curtis auf dem Keller, Ulrich McCormick, Siobhan Austin, Pamela Overall, Christopher M. Adam, Michael J. Ruth, Thomas J. Perrin, David M.},
	month = {Sep},
	pages = {12045-12055},
	type = {Article},
	abstract = {The use of a boronic ester as a captor of aqueous [F-18]-fluoride has been previously suggested as a means of labeling biomolecules in one step for positron emission tomography (PET) imaging. For this approach to be seriously considered, the [F-18]-labeled trifluoroborate should be humorally stable such that it neither leaches free [F-18]-fluoride to the bone nor accumulates therein. Herein, we have synthesized a biotinylated boronic ester that is converted to the corresponding trifluoroborate salt in the presence of aqueous [F-18]-fluoride. In keeping with its in vitro aqueous kinetic stability at pH 7.5, the trifluoroborate appears to clear in vivo quite rapidly to the bladder as the stable trifluoroborate salt with no detectable leaching of free [F-18]-fluoride to the bone. When this labeled biotin is preincubated with avidin, the pharmacokinetic clearance of the resulting complex is visibly altered. This work validates initial claims that boronic esters are potentially useful as readily labeled precursors to [F-18]-PET reagents.},
	keywords = {apoptosis, BIODISTRIBUTION, CANCER, DESIGN, F-18, MICROPET, NO-CARRIER, PEPTIDES, PET, STABILITY},
	isbn = {0002-7863},
	url = {<Go to ISI>://000258950500044},
	author = {Ting, R. and Harwig, C. and auf dem Keller, U. and McCormick, S. and Austin, P. and Overall, C. M. and Adam,Michael J. and Ruth, T. J. and Perrin,David M.}
}
@article {1483,
	title = {Coulomb effects in binding of heme in gas-phase ions of myoglobin},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {20},
	number = {2},
	year = {2006},
	note = {ISI Document Delivery No.: 003PGTimes Cited: 3Cited Reference Count: 31},
	pages = {111-117},
	type = {Article},
	abstract = {Coulomb effects in binding of heme in gas-phase holomyoglobin ions are studied. Positive and negative ions are formed from solution myoglobin with Fe2+ (ferromyoglobin) and Fe3+ (ferrimyoglobin). The energy that must be added to the resulting holomyoglobin ions to cause heme loss has been measured by triple-quadrupole tandem mass spectrometry. With negative ions, neutral heme is lost regardless of the charge state of Fe in solution. It is likely that the Fe3+ is reduced to Fe2+ in the negative electrospray process. With positive ions, predominantly neutral heme loss is observed with ions formed from ferromyoglobin in solution, and positive heme loss with ions formed from ferrimyoglobin in solution. The energies required to induce neutral heme loss are similar for positive and negative ions. The energies required to induce charged heme loss from positive holomyoglobin ions are significantly less. Coulomb repulsion between the charged heme and charged protein appears to lower the barrier for heme loss. These results are consistent with a simple model potential with a long-range Coulomb repulsion and short-range attraction between the heme and protein. Copyright (c) 2005 John Wiley \& Sons, Ltd.},
	keywords = {B(5), COLLISION CROSS-SECTIONS, CYTOCHROME, DISSOCIATION, ELECTROSTATIC INTERACTIONS, GLOBIN COMPLEXES, HOLOMYOGLOBIN, IONIZATION-MASS-SPECTROMETRY, PROTEINS, STABILITY, ZN-MYOGLOBIN},
	isbn = {0951-4198},
	url = {<Go to ISI>://000234693500006},
	author = {Mark, K. J. and Douglas, D. J.}
}
@article {1555,
	title = {Engineering proteins with novel mechanical properties by recombination of protein fragments},
	journal = {Angewandte Chemie-International Edition},
	volume = {45},
	number = {34},
	year = {2006},
	note = {ISI Document Delivery No.: 082MRTimes Cited: 20Cited Reference Count: 51Sharma, Deepak Cao, Yi Li, Hongbin},
	pages = {5633-5638},
	type = {Article},
	keywords = {AFM, ATOMIC-FORCE MICROSCOPY, ELASTICITY, EVOLUTION, IG DOMAIN, IMMUNOGLOBULIN DOMAINS, MOLECULAR-DYNAMICS SIMULATIONS, protein engineering, protein structures, scanning probe microscopy, SINGLE PROTEIN, single-molecule studies, SPECTROSCOPY, STABILITY, TITIN},
	isbn = {1433-7851},
	url = {<Go to ISI>://000240391400016},
	author = {Sharma, D. and Cao, Y. and Li, H. B.}
}
@article {713,
	title = {Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens},
	journal = {Carbohydrate Research},
	volume = {338},
	number = {5},
	year = {2003},
	note = {ISI Document Delivery No.: 645XBTimes Cited: 6Cited Reference Count: 38},
	month = {Feb},
	pages = {415-421},
	type = {Article},
	abstract = {The xylanase, BadX, from the alkalophilic Bacillus agaradhaerens was cloned, expressed and studied in comparison to a related family 11 xylanase, BcX, from B. circulans. Despite the alkaline versus neutral conditions under which these bacteria grow, BadX and BcX both exhibit optimal activity near pH 5.6 using the substrate omicron-nitrophenyl beta-xylobioside. Analysis of the bell-shaped activity profile of BadX yielded apparent pK(a) values of 4.2 and 7.1, assignable to its nucleophile Glu94 and general acid Glu184, respectively. In addition to having an similar to 10-fold higher k(cat)/K-m value with this substrate at pH 6 and 40 degreesC, BadX has significantly higher thermal stability than BcX under neutral and alkaline conditions. This enhanced stability, rather than a shift in its pH-optimum, may allow BadX to hydrolyze xylan under conditions of elevated temperature and pH. (C) 2003 Elsevier Science Ltd. All rights reserved.},
	keywords = {bacillus xylanase, CIRCULANS XYLANASE, CLASSIFICATION, electrostatic, extremophile, glycosidase, GLYCOSYL-ENZYME INTERMEDIATE, HYDROLASES, interactions, NMR ASSIGNMENTS, pH-dependent mechanism, PK(A), PROTEIN, STABILITY, THERMOSTABILITY},
	isbn = {0008-6215},
	url = {<Go to ISI>://000181004800004},
	author = {Poon, D. K. Y. and Webster, P. and Withers, S. G. and McIntosh, L. P.}
}
@article {342,
	title = {A comparison of three- and four-helix bundle TASP molecules},
	journal = {Journal of Peptide Science},
	volume = {8},
	number = {6},
	year = {2002},
	note = {ISI Document Delivery No.: 563ZTTimes Cited: 14Cited Reference Count: 19},
	month = {Jun},
	pages = {275-282},
	type = {Article},
	abstract = {We have designed, synthesized and characterized three- and four-helix bundle template-assembled synthetic proteins (TASPs). The TASPs were synthesized using disulphide bonds between the peptides and either the cyclotribenzylene (CTB) template, or the cavitand (BOWL) template, to form the three- and four helix bundles, respectively. The TASPs were constructed using peptides that were linked via their N-termini (peptide CGGGEELLKKXEELLKKG, where X = L, I, Nle or V), or via their C-termini (peptide GEELLKKLEELLKKGGGC). Each TASP was assayed for its structure, stability, {\textquoteright}native-like{\textquoteright} characteristics and whether it was a monomer in solution. All TASPs were found to be highly helical, and highly resistant to chemical denaturation using guanidine hydrochloride (GnHCl). Analysis of the GnHCl-induced unfolding curves of the different TASPs demonstrated stability differences based on the number of helices in the bundle, the end of the helix that was attached to the template, and the identity of the core amino acid. The TASPs all had molten-globule structure, which is (generally) consistent with a degenerate sequence in the core. The four-helix bundle TASPs appeared to be monomers in solution, whereas there is some evidence that the three-helix bundle TASPs are weakly self associating. Copyright. (C) 2002 European Peptide Society and John Wiley Sons, Ltd.},
	keywords = {4-HELIX BUNDLES, DESIGN, four-helix bundle, PROTEIN, STABILITY, TASP, template assembled synthetic protein, three-helix bundle},
	isbn = {1075-2617},
	url = {<Go to ISI>://000176289000005},
	author = {Causton, A. S. and Sherman, J. C.}
}
@article {439,
	title = {Hydrogen/deuterium exchange of myoglobin ions in a linear quadrupole ion trap},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {16},
	number = {20},
	year = {2002},
	note = {ISI Document Delivery No.: 604ADTimes Cited: 10Cited Reference Count: 26},
	pages = {1941-1945},
	type = {Article},
	abstract = {The hydrogen/deuterium (H/D) exchange of gas-phase ions of holo- and apo-myoglobin has been studied by confining the ions in a linear quadrupole ion trap with D2O or CD3OD at a pressure of several mTorr. Apo-myoglobin ions were formed by collision-induced dissociation of holomyoglobin ions between the orifice and skimmer of the ion sampling system. The exchange takes place on a time scale of seconds. Earlier cross section measurements have shown that holomyoglobin ions can have more compact structures than apo-myoglobin. Despite this, both holomyoglobin and apo-myoglobin in charge states +8 to +14 are found to exchange nearly the same number of hydrogens (ca. 103) in 4 s. It is possible the ions fold or unfold to new conformations on the much longer time scale of the exchange experiment compared with the cross section measurements. Copyright (C) 2002 John Wiley Sons, Ltd.},
	keywords = {COLLISION CROSS-SECTIONS, CYTOCHROME-C, GAS-PHASE, HEME, HOLOMYOGLOBIN, HYDROGEN-DEUTERIUM EXCHANGE, MASS-SPECTROMETRY, OF-FLIGHT, PROTEIN IONS, STABILITY, SYSTEM},
	isbn = {0951-4198},
	url = {<Go to ISI>://000178592700007},
	author = {Mao, D. M. and Ding, C. F. and Douglas, D. J.}
}
@article {540,
	title = {The microwave spectrum and structure of KrAgF},
	journal = {Journal of Molecular Structure},
	volume = {612},
	number = {2-3},
	year = {2002},
	note = {ISI Document Delivery No.: 573UATimes Cited: 22Cited Reference Count: 27Sp. Iss. SI},
	month = {Jul},
	pages = {109-116},
	type = {Article},
	abstract = {The microwave spectrum of KrAgF has been assigned between 8-18 GHz, using a cavity pulsed-jet Fourier transform microwave spectrometer. The structure of the molecule has been calculated from the measured rotational constants of four isotopomers. Values for the Kr-Ag and Ag-F bond lengths of similar to2.594 and similar to1.957 Angstrom respectively have been determined. A small centrifugal distortion constant (similar to0.3 kHz) indicates that the molecule is comparatively rigid. The stretching frequency and dissociation energy of the Kr-Ag bond have been subjected to ab initio calculation at the MP2 level, yieling results of similar to113 cm(-1) and similar to32 kJ mol(-1) respectively. A Mulliken orbital population analysis suggests that the Kr-Ag bond is weakly covalent in nature. All parameters are found to be consistent with trends established for ArMX and KrMX species. (C) 2002 Elsevier Science B.V. All rights reserved.},
	keywords = {ab initio calculation, CL, CONSTANTS, CORRELATED MOLECULAR CALCULATIONS, GAUSSIAN-BASIS SETS, HYPERFINE, KR, microwave spectrum, STABILITY, structure of KrAgF},
	isbn = {0022-2860},
	url = {<Go to ISI>://000176848500006},
	author = {Walker, N. R. and Reynard, L. M. and Gerry, M. C. L.}
}
@article {5045,
	title = {Determination of trivalent methylated arsenicals in biological matrices},
	journal = {Toxicology and Applied Pharmacology},
	volume = {174},
	number = {3},
	year = {2001},
	note = {ISI Document Delivery No.: 464KTTimes Cited: 129Cited Reference Count: 67},
	month = {Aug},
	pages = {282-293},
	type = {Article},
	abstract = {The enzymatically catalyzed oxidative methylation of As yields methylated arsenicals that contain pentavalent As (As-V). Because trivalent As (As-III) is the favored substrate for this methyltransferase, methylated arsenicals containing As-V are reduced to trivalency in cells. Methylated arsenicals that contain As-III are extremely potent inhibitors of NADPH-dependent flavoprotein oxidoreductases and potent cytotoxins in many cell types. Therefore, the formation of methylated arsenicals that contain As-III may be properly regarded as an activation step, rather than a means of detoxification. Recognition of the role of methylated arsenicals that contain As-III in the toxicity and metabolism of As emphasizes the need for analytical methods to detect and quantify these species in biological samples. Hence, a method was developed to exploit pH-dependent differences in the generation of arsines from inorganic and methylated arsenicals that contain either As-V or As-III. Reduction with borohydride at pH 6 generated arsines from inorganic As-III, methyl As-III, and dimethyl As-III, but not from inorganic As-V, methyl As-V, and dimethyl As-V. Reduction with borohydride at pH 2 or lower generated arsines from arsenicals that contained either As-V or As-III. Arsines are trapped in a liquid nitrogen-cooled gas chromatographic trap, which is subsequently warmed to allow separation of the hydrides by their boiling points. Atomic absorption spectrophotometry is used to detect and quantify the arsines. The detection limits (ng As ml(-1)) for inorganic As-III, methyl As-III, and dimethyl As-III are 1.1, 1.2, and 6.5, respectively. This method has been applied to the analysis of arsenicals in water, human urine, and cultured cells. Both methyl As-III. and dimethyl As-III are detected in urine samples from individuals who chronically consumed inorganic As-contaminated water and in human cells exposed in vitro to inorganic As-III. The reliable quantitation of inorganic and methylated arsenicals that contain As-III. in biological samples will aid the study of the toxicity of these species and may provide a new biomarker of the effects of chronic exposure to As. (C) 2001 Academic Press.},
	keywords = {analysis, arsenic, atomic absorption spectrophotometry, biological matrices, CANCER MORTALITY, DIABETES-MELLITUS, DIMETHYLARSINIC ACID, DOSE-RESPONSE RELATIONSHIP, DRINKING-WATER, ENZYMATIC, HUMAN URINE, HYDRIDE GENERATION, MAMMALIAN SYSTEMS, MASS-SPECTROMETRY, METABOLISM, methylated arsenic, METHYLATION, MONOMETHYLARSONOUS ACID MMA(III), pentavalent arsenic, STABILITY, TOXICITY, trivalent arsenic},
	isbn = {0041-008X},
	url = {<Go to ISI>://000170532300010},
	author = {Del Razo, L. M. and Styblo, M. and Cullen, W. R. and Thomas, D. J.}
}
@article {5202,
	title = {Effects of sequential replacement of -NH2 by -OH in the tripodal tetraamine tren on its acidity and metal ion coordinating properties},
	journal = {Inorganic Chemistry},
	volume = {40},
	number = {7},
	year = {2001},
	note = {ISI Document Delivery No.: 413ATTimes Cited: 26Cited Reference Count: 32},
	month = {Mar},
	pages = {1527-1535},
	type = {Article},
	abstract = {The preparation is described of two modified derivatives of the tripodal tetraamine tren, 2-hydroxy-N,N-bis(2-aminoethyl)ethylamine, NNO(2)222, and 2-amino-N,N-bis(2-hydroxyethyl)ethylamine NNO(2)222, in which one and two primary amines, respectively, have been replaced with hydroxyl groups. The aqueous acid-base and metal ion (Ni2+, Cu2+: Zn2+ coordination properties of these two compounds were studied by potentiometric, spectrophotometric, and NMR titrations. Two and three acidity constants, respectively, were determined for NNO(2)222 and NN(2)O222 by potentiometry. NMR titrations proved that deprotonation of the two OH residues in NNO(2)222, and of the one in NN(2)O222, corresponded to pK(a) > 14. Acidity constants related to deprotonation-of the terminal primary amine functions were similar in both NNO2222 and NN(2)O222 land to those in the parent compound tren), whereas deprotonation of the tertiary ammonium N atom had a very different acidity constant in each of these three compounds. Charge repulsion, polar effects, and intramolecular hydrogen bond formation an responsible for the discrepancy. Chelated diamine metal complexes for each ligand studied depended only on the basicity of the corresponding two amines, suggesting that the hydroxyl group interacted with the metal ion very weakly in acidic or neutral solutions. The ML2+ species further deprotonated to form M(L - H)(+) and M(L - 2H) complexes, in which the protons are released from the coordinated OH group. A pM vs pH correlation showed that replacing an NH2 group with a OH group in tren or NN(2)O222 makes the resulting metal complex less stable. Electronic spectra showed that the Cu(II) complexes of both NNO(2)222 and NN(2)O222 adopted a square pyramidal geometry rather than a trigonal bipyramidal geometry. The X-ray crystal structure analysis of the zinc complex [Zn(OH)(mu -NNO(2)222 - H)Zn(NNO(2)222)](2+), as its [BF4](-) salt, shows a dinuclear molecule containing two zinc ions, each coordinated in a distorted trigonal bipyramid. The coordination environment at one zinc atom is composed of the four donor groups of a mono-O-deprotonated ligand NNO(2)222 and a hydroxyl ion with the central nitrogen atom of the ligand and the hydroxyl ion in equatorial positions. The oxygen atom of the deprotonated alkoxo group bridges to the second zinc atom, which is coordinated by this atom and one undeprotonated ligand NNO2222.},
	keywords = {COPPER(II) COMPLEXES, CRYSTAL, DIPERCHLORATE, donor ligands, STABILITY},
	isbn = {0020-1669},
	url = {<Go to ISI>://000167588300019},
	author = {Song, B. and Reuber, J. and Ochs, C. and Hahn, F. E. and Lugger, T. and Orvig, Chris}
}
@article {5173,
	title = {Microwave spectrum, structure, and hyperfine constants of Kr-AgCl: Formation of a weak Kr-Ag covalent bond},
	journal = {Journal of Molecular Spectroscopy},
	volume = {206},
	number = {1},
	year = {2001},
	note = {ISI Document Delivery No.: 428BNTimes Cited: 29Cited Reference Count: 38},
	month = {Mar},
	pages = {33-40},
	type = {Article},
	abstract = {The pure rotational spectrum of the complex Kr-AgCl has been measured between 8-15 GHz using a cavity pulsed-jet Fourier transform microwave spectrometer. The complex was found to be linear and relatively rigid, with a Kr-Ag bond length of similar to2.641 Angstrom. The Kr-Ag stretching frequency was estimated to be 117 cm(-1). Ab initio calculations performed at the MP2 level of theory gave the geometry, vibration frequencies, Kr-Ag bond dissociation energy, and orbital populations. The Kr-Ag bond dissociation energy was estimated to be -28 kJ mol(-1). The Kr-Ag force constant and dissociation energy are greater than those of Ar-Ag in Ar-AgCl. The chlorine nuclear quadrupole coupling constants show slight changes on complex formation. Ab initio orbital population analysis shows a small shift in sigma -electron density from Kr to Ag on complex formation. The combined experimental and ab initio results are consistent with the presence of a weak Kr-Ag covalent bond. (C) 2001 Academic Press},
	keywords = {ATOMS, COMPLEXES, CORRELATED MOLECULAR CALCULATIONS, DER-WAALS, FOURIER-TRANSFORM SPECTROSCOPY, GAUSSIAN-BASIS SETS, LASER-ABLATION, RAMAN, ROTATIONAL SPECTRUM, STABILITY, TRANSITION-METAL COMPLEXES},
	isbn = {0022-2852},
	url = {<Go to ISI>://000168441400004},
	author = {Reynard, L. M. and Evans, C. J. and Gerry, M. C. L.}
}
@article {5231,
	title = {[ReO(N2O2)X] complexes: "4+1"?},
	journal = {Inorganic Chemistry},
	volume = {40},
	number = {18},
	year = {2001},
	note = {ISI Document Delivery No.: 466JNTimes Cited: 3Cited Reference Count: 36},
	month = {Aug},
	pages = {4623-4626},
	type = {Article},
	abstract = {{[ReO(ppme)X] (where ppme(2-) is 2,5-diazo-N,N {\textquoteright} -dimethylhexyl-1,6-bis(phenylphosphinate)},
	keywords = {CHEMISTRY, OXO-COMPLEXES, PEPTIDES, RADIOPHARMACEUTICALS, RHENIUM(V), SCHIFF-BASE LIGANDS, STABILITY, TC-99M, TECHNETIUM COMPLEXES, X-ray structures},
	isbn = {0020-1669},
	url = {<Go to ISI>://000170642600019},
	author = {Xu, L. and Lowe, M. P. and Rettig, S. J. and Orvig, Chris}
}
@article {4848,
	title = {Crystallization of dipolar spheres: A discussion of second-order density functional theory},
	journal = {Journal of Chemical Physics},
	volume = {112},
	number = {24},
	year = {2000},
	note = {ISI Document Delivery No.: 324HYTimes Cited: 6Cited Reference Count: 43},
	month = {Jun},
	pages = {10949-10956},
	type = {Article},
	abstract = {We investigate the application of second-order density functional theory to the crystallization of dipolar hard and soft spheres. It is shown that the results are highly sensitive to the repulsive part of the pair potential, and to the symmetry of the fluid phase considered in the density functional theory. In general, the theoretical results for dipolar soft spheres (with r(-12) repulsion) are found to be physically more reasonable than those obtained for dipolar hard spheres. In particular, the fluid-solid density gap is greatly reduced and lies in the range expected on physical grounds and from simulations. However, theories constructed by expanding about the isotropic fluid phase overestimate the stability of the ferroelectric solid for both models, and fail to predict the stable ferroelectric fluids found in computer simulations. We have carried out calculations using ferroelectric dipolar fluids with both perfect and fluctuating orientational order as "starting points" in the density functional expansion. The results demonstrate the high sensitivity of the theory to the underlying fluid state, and strongly indicate the existence of stable ferroelectric fluids in accord with computer simulations. (C) 2000 American Institute of Physics. [S0021-9606(00)50924-6].},
	keywords = {FLUIDS, HARD-SPHERES, INTEGRAL-EQUATIONS, LIQUID-VAPOR INTERFACE, NEMATIC PHASE, orientational order, PHASE-TRANSITIONS, SOFT SPHERES, SOLID-PHASES, STABILITY},
	isbn = {0021-9606},
	url = {<Go to ISI>://000087617300033},
	author = {Klapp, S. H. L. and Patey, G. N.}
}
@article {4617,
	title = {Cavitands are effective templates for inducing stability and nativelike structure in de Novo four-helix bundles},
	journal = {Journal of the American Chemical Society},
	volume = {121},
	number = {39},
	year = {1999},
	note = {ISI Document Delivery No.: 243QXTimes Cited: 40Cited Reference Count: 92},
	month = {Oct},
	pages = {8983-8994},
	type = {Article},
	abstract = {We have designed, synthesized and characterized eight cavitand-based de novo four-helix bundles, where each helix contains the basis sequence EELLKKLEELLKKG. We find that each de novo protein is highly helical and extremely stable to the chemical denaturant guanidine hydrochloride (GuHCl). We studied the effect of the cavitand-peptide linker on the stability of each de novo protein. Flexible linkers render the helical structures more susceptible to denaturation by GuHCl. Linker structure and length also dictate monomer/dimer equilibria of the proteins. Proteins containing 0-3 Cry units possess varying degrees of nativelike structure. In contrast, proteins containing two or four methylene Linkers are more characteristic of molten globules. These differences can be attributed to the additional hydrogen bonding capabilities of the glycine linker variants and to the distance between the cavitand template and the helical bundle. The cavitand pendent group was also changed in one de novo protein from a methyl group to a propyl-phosphate moiety. This alteration does not affect the stability or packing within the helical bundle; however, it does affect the monomer/dimer equilibrium.},
	keywords = {4-HELIX BUNDLE, ASSEMBLED, conformational, DESIGNED PROTEIN, HOST GUEST COMPLEXATION, HYDROGEN-EXCHANGE, MOLTEN GLOBULE, NONPOLAR AMINO-ACIDS, rational design, STABILITY, SYNTHETIC PROTEINS, ULTRAVIOLET CIRCULAR-DICHROISM},
	isbn = {0002-7863},
	url = {<Go to ISI>://000083009700003},
	author = {Mezo, A. R. and Sherman, J. C.}
}
@article {4365,
	title = {Conformation of native, reduced and [5-55](Ala) bovine pancreatic trypsin inhibitor in the gas phase},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {12},
	number = {1},
	year = {1998},
	note = {ISI Document Delivery No.: YQ873Times Cited: 14Cited Reference Count: 46},
	pages = {40-44},
	type = {Article},
	abstract = {Collision cross sections have been measured for gas phase ions of native oxidized bovine pancreatic trypsin inhibitor (BPTI), native reduced BPTI and a mutant form of BPTI containing a single disulphide bond between residues 5 and 55 ([5-55](Ala) BPTI). Cross sections for [5-55](Ala) BPTI and reduced BPTI were 9\% and 17\% greater respectively than those for native BPTI, Cross sections for native BPTI were smaller than previous estimates from the crystal structure but in reasonable agreement with values calculated from the radius of gyration determined by x-ray scattering from solution BPTI. The increase in cross section for reduced BPTI over native BPTI is similar to that seen in molecular dynamics simulations, The results show that the disulphide bonds of BPTI contribute to the folding of the gas phase ions, but that even in the absence of disulphide bonds the protein ions maintain compact structures. Comparisons to relative areas calculated from hydrodynamic radii of BPTI in solution suggest that when disulphide linkages are removed, BPTI in the gas phase unfolds less than BPTI in solution. (C) 1998 John Wiley \& Sons, Ltd.},
	keywords = {BPTI, DISULFIDE BOND, IONS, MASS-SPECTROMETRY, MOLECULAR-DYNAMICS SIMULATIONS, MYOGLOBIN, protein dynamics, STABILITY},
	isbn = {0951-4198},
	url = {<Go to ISI>://000071433000008},
	author = {Nesatiy, V. and Chen, Y. L. and Collings, B. A. and Douglas, D. J.}
}
@article {4336,
	title = {Tightening the hydrophobic belt: Effects of backbone and donor group variation on podand ligand complexes of the lanthanides},
	journal = {Inorganic Chemistry},
	volume = {37},
	number = {7},
	year = {1998},
	note = {ISI Document Delivery No.: ZG944Times Cited: 44Cited Reference Count: 53},
	month = {Apr},
	pages = {1637-1647},
	type = {Article},
	abstract = {{The N4O3 tripodal aminomethylene phosphinato ligand tris(4-phenylphosphinato-3-methyl-3-azabutyl)amine (H-3-ppma) forms mono- and bis(ligand) complexes with lanthanide(III) metal ions Ln when Ln = Sm-Lu. The formation constants of the Lu (log beta(1) = 1.79, log beta(2) = 4.40) and the Yb (log beta(1) = 2.25, log beta(2) = 4.42) complexes were determined at pH = 1.5 using an unusual P-31 NMR spectroscopic method. The molecular structure of the lutetium complex [Lu(H(3)ppma)(2)](NO3)(3) . 3H(2)O (C60H96LuN11O24P6) was solved by X-ray methods; it crystallizes in the trigonal space group R(3) over barc$, with a = 19.060(1) Angstrom},
	keywords = {AMINE PHENOL LIGANDS, BIOLOGICAL-SYSTEMS, CHEMISTRY, COORDINATION, DESIGN, HEPTADENTATE LIGANDS, METAL-IONS, NMR SHIFTS, NUCLEAR MAGNETIC-RESONANCE, STABILITY},
	isbn = {0020-1669},
	url = {<Go to ISI>://000073055700034},
	author = {Lowe, M. P. and Caravan, P. and Rettig, S. J. and Orvig, Chris}
}
@article {4290,
	title = {Tripodal trisamides based on nicotinic and picolinic acid derivatives},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {76},
	number = {4},
	year = {1998},
	note = {ISI Document Delivery No.: 101TQTimes Cited: 6Cited Reference Count: 46},
	month = {Apr},
	pages = {414-425},
	type = {Article},
	abstract = {{A number of polydentate arylamide ligands have been prepared by coupling various acyclic tripodal or linear polyamines with derivatives of nicotinic and picolinic acids. Two synthetic procedures were utilized; tris {[(2-hydroxynicotinyl)carbonyl]-2-aminoethyl} (H3NICTREN) was prepared by Method A, the HOSu/DCC method, and the other arylamides in this study were prepared by Method B, the CDI method. Method A involved the reaction of N-hydroxysuccinimide with 2-hydroxynicotinic acid (in the presence of dicyclohexylcarbodiimide (DCC) as a dehydrative coupling reagent) to form the succinimide ester, followed by reaction with TREN to yield H3NICTREN. Method B involved reaction of a carboxylic acid (2-hydroxynicotinic, 3-hydroxypicolinic, nicotinic, or picolinic acids) with carbonyldiimidazole (CDI) to form the N-acylimidazolide, followed by reaction with the amine (TREN, TAME, spermidine, or TRPN) to yield the desired arylamide. The X-ray structure of 1,1,1-tris{[(3 -hydroxypicolinyl) carbonyl] -2-aminomethyl} ethane (H3PICTBME) was determined; crystals of H(3)PICTAME are monoclinic},
	keywords = {aluminum, arylamide, CHELATE COMPLEXES, COORDINATION CHEMISTRY, DISTANCES, ENTEROBACTIN ANALOGS, FERRIC ENTEROBACTIN, gallium, hydrogen bonding, MICROBIAL IRON TRANSPORT, NEUTRAL WATER, preorganization, STABILITY},
	isbn = {0008-4042},
	url = {<Go to ISI>://000074884600007},
	author = {Hoveyda, H. R. and Karunaratne, V. and Nichols, C. J. and Rettig, S. J. and Stephens, A. K. W. and Orvig, Chris}
}
@article {4030,
	title = {Acid-induced denaturation of myoglobin studied by time-resolved electrospray ionization mass spectrometry},
	journal = {Biochemistry},
	volume = {36},
	number = {21},
	year = {1997},
	note = {ISI Document Delivery No.: XB321Times Cited: 74Cited Reference Count: 43},
	month = {May},
	pages = {6448-6454},
	type = {Article},
	abstract = {The acid-induced denaturation of holo-myoglobin (hMb) following a pH-jump from 6.5 to 3.2 has been studied by electrospray ionization (ESI) mass spectrometry in combination with a continuous flow mixing technique (time-resolved ESI MS). Different protein conformations are detected by the different charge state distributions that they generate during ESI. The changes in intensity of the peaks in the mass spectrum as a function of time can be described by two exponential lifetimes of 0.38 +/- 0.06 s and 6.1 +/- 0.5 s, respectively. The acid-induced denaturation of hMb was also studied in stopped-flow experiments by monitoring changes in the Soret absorption. The lifetimes measured by this method are in good agreement with those obtained by time-resolved ESI MS. The shorter lifetime is associated with the formation of a transient intermediate which shows the mass of the intact heme-protein complex but leads to the formation of much higher charge states during ESI than native hMb at pH 6.5. This form of hMb has an absorption spectrum similar to that of the native protein, indicating a relatively unperturbed chromophore environment inside the heme binding pocket. The intermediate can thus be characterized as an unfolded form of hMb with essentially intact heme-protein interactions. The longer of the two lifetimes is associated with the formation of a product which has a blue-shifted absorption spectrum with a much lower maximum absorption coefficient than observed for native hMb. In the ESI mass spectrum, this product appears as the apoprotein with high charge states which indicates the disruption of the native heme-protein interactions and a considerable degree of unfolding compared to native apo-myoglobin. The mechanism of acid-induced denaturation of hMb, therefore, appears to follow the sequence (heme protein)(native) {\textendash}> (heme-protein)(unfolded) {\textendash}> heme + (protein)(unfolded).},
	keywords = {APOMYOGLOBIN, HEME-PROTEINS, INTERMEDIATE, IONS, LOW PH, METMYOGLOBIN, PROBING CONFORMATIONAL-CHANGES, RESOLUTION, SPERM WHALE, STABILITY},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1997XB32100022},
	author = {Konermann, L. and Rosell, F. I. and Mauk, A. G. and Douglas, D. J.}
}
@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 {3928,
	title = {Effect of pyridyl donors in the chelation of aluminum(III), gallium(III), and indium(III)},
	journal = {Inorganic Chemistry},
	volume = {36},
	number = {7},
	year = {1997},
	note = {ISI Document Delivery No.: WQ490Times Cited: 18Cited Reference Count: 62},
	month = {Mar},
	pages = {1306-1315},
	type = {Article},
	abstract = {{A new preparation of N,N{\textquoteright}-bis(2-pyridylmethyl)ethylenediamine-N,N{\textquoteright}-diacetic acid (H(2)bped) is reported, and its properties of complexation with Al(III), Ga(III), In(III), and Co(III) are investigated. The molecular structure of the cobalt(III) complex [Co(bped)]PF6 . CH3CN . H2O (C20H25CoF6N5O5P) has been solved by X-ray methods; the complex crystallizes in the triclinic space group P (1) over bar, with a = 10.611(2) Angstrom},
	keywords = {AQUEOUS-SOLUTION, BINDING CONSTANTS, COMPLEXES, COORDINATION, CRYSTAL-STRUCTURES, LIGANDS, METAL-IONS, MULTINUCLEAR MAGNETIC-RESONANCE, N, N{\textquoteright}-BIS(2-HYDROXYBENZYL)ETHYLENEDIAMINE-N, N{\textquoteright}-DIACETIC ACID, STABILITY},
	isbn = {0020-1669},
	url = {<Go to ISI>://A1997WQ49000006},
	author = {Caravan, P. and Rettig, S. J. and Orvig, Chris}
}
@article {3860,
	title = {Study of a commercial SiO2 sol and gel by small angle x-ray scattering: Effect of sample thickness and interpretation by means of smoluchowski scheme},
	journal = {Clays and Clay Minerals},
	volume = {44},
	number = {2},
	year = {1996},
	note = {ISI Document Delivery No.: UL994Times Cited: 4Cited Reference Count: 35},
	month = {Apr},
	pages = {197-213},
	type = {Article},
	abstract = {Ludox HS SiO2 sols at high concentrations show a peak in small angle x-ray scattering (SAXS) reminiscent to a {\textquoteright}{\textquoteright}structure.{\textquoteright}{\textquoteright} The appearance of such a peak was found to depend crucially on the thickness of the sample cell used for SAXS measurements. The thinner the cell used, the more prominent the peak. When the thickness was larger than 2 mm, it was no longer observable. When sols were treated with activated charcoal powders (in order to remove a surfactant) the peak became less prominent. For the cases where clear features for structure were absent (thick sample regime), the Smoluchowski scheme was utilized to study the nature of sols. Namely, the distribution of the Smoluchowski species were estimated by numerically calculating the size distribution of particles directly from SAXS data. The distribution was found basically bimodal, and the main distribution peak, particularly for dilute sols (less than 5 wt\%), was consistent with primary particles of SiO2. The second distribution peak was strongly dependent on the concentration of SiO2 particles. The observed trend was that the higher the concentration of SiO2 particles, the more prominent the second distribution peak and the locus of the maximum tended to move toward a smaller value in diameter. This behavior of the second distribution peak of the Smoluchowski species is no doubt a manifestation of the interparticle correlation. The observation of such behavior may provide a convenient means to characterize sols with interparticle correlation. This method was also applied for characterizing gels formed when the pH values were altered.},
	keywords = {COLLOIDAL SILICA, dependence of sample thickness, Ludox HS SiO2, MIXTURES, MULTIPLE-SCATTERING, NEUTRON-SCATTERING, SAXS, SCHEME, Smoluchowski, STABILITY, structure in sol, SYSTEMS, WATER},
	isbn = {0009-8604},
	url = {<Go to ISI>://A1996UL99400005},
	author = {Xu, Y. N. and Hiew, P. L. and Klippenstein, M. A. and Koga,Yoshikata}
}
@article {2994,
	title = {GROUND-STATE CONFIGURATIONS OF MODEL MOLECULAR CLUSTERS},
	journal = {Journal of Chemical Physics},
	volume = {100},
	number = {3},
	year = {1994},
	note = {ISI Document Delivery No.: MU316Times Cited: 24Cited Reference Count: 32},
	month = {Feb},
	pages = {2213-2219},
	type = {Article},
	abstract = {We have determined the ground state configurations of model molecular dipolar clusters using Monte Carlo simulations. Cluster sizes ranged from N=3 to N=20. The molecular models consisted of spherically symmetric hard sphere or Lennard-Jones interactions, as well as dipole-dipole, dipole-quadrupole, and quadrupole-quadrupole interactions. Molecular polarizability was also included in some calculations. We first found the ground state configurations of dipolar hard sphere clusters, and then systematically increased the quadrupole moment and molecular polarizability from zero up to typical values for small molecules. The relevance of our results to real molecular clusters is discussed.},
	keywords = {COMPUTATIONS, DYNAMICS, HYDROGEN-FLUORIDE CLUSTERS, LENNARD-JONES CLUSTERS, LIQUID, MONTE-CARLO, OPTIMIZATION, SIMULATION, STABILITY},
	isbn = {0021-9606},
	url = {<Go to ISI>://A1994MU31600043},
	author = {Clarke, A. S. and Patey, G. N.}
}
@article {2704,
	title = {CHARACTERIZATION OF SPUTTER DEPOSITED INCONEL CARBON X-RAY MULTILAYERS},
	journal = {Journal of Vacuum Science \& Technology a-Vacuum Surfaces and Films},
	volume = {11},
	number = {1},
	year = {1993},
	note = {ISI Document Delivery No.: KH557Times Cited: 4Cited Reference Count: 25},
	month = {Jan-Feb},
	pages = {115-124},
	type = {Article},
	abstract = {The reflectivity of x-ray multilayers made of new pairs of materials was theoretically calculated at a wavelength of 45 angstrom. Carbon and inconel were then selected for {\textquoteright}{\textquoteright}low index{\textquoteright}{\textquoteright} and {\textquoteright}{\textquoteright}high index{\textquoteright}{\textquoteright} layers, respectively, in the multilayer system. Single layers, bilayers, and multilayers of carbon and inconel were characterized by grazing x-ray reflectometry (GXR), x-ray photoelectron spectroscopy (XPS), Auger electron spectroscopy (AES), and spectroscopic ellipsometry (SE). From GXR data at 1.54 angstrom refractive indices and film thicknesses of inconel and carbon layers were obtained. From an analysis of SE data, the dielectric function and the thickness as of inconel and carbon thin films were deduced. XPS and AES measurements revealed the presence of carbides at the interface between carbon and inconel. GXR analysis was performed on ten-layer C/inconel multilayers. The GXR interference pattern was found to broaden after annealing the samples at 600-degrees-C.},
	keywords = {CARBIDE, FILMS, OPTICS, SI, STABILITY},
	isbn = {0734-2101},
	url = {<Go to ISI>://A1993KH55700015},
	author = {Aouadi, M. S. and Parsons, R. R. and Wong, P. C. and Mitchell, K. A. R.}
}
@article {2925,
	title = {CIRCULAR-DICHROISM ANALYSIS OF A SYNTHETIC PEPTIDE CORRESPONDING TO THE ALPHA,ALPHA-CORNER MOTIF OF HEMOGLOBIN},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {196},
	number = {1},
	year = {1993},
	note = {ISI Document Delivery No.: MC105Times Cited: 1Cited Reference Count: 16},
	month = {Oct},
	pages = {435-439},
	type = {Article},
	keywords = {ALPHA-HELIX, GLOBULAR-PROTEINS, INTERMEDIATE, POLYPEPTIDE-CHAIN, SECONDARY STRUCTURE, STABILITY},
	isbn = {0006-291X},
	url = {<Go to ISI>://A1993MC10500062},
	author = {Tsai, F. C. S. and Sherman, J. C.}
}
@article {7148,
	title = {THE CRYSTAL AND MOLECULAR-STRUCTURE OF GOLD TRIS(FLUOROSULFATE)},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {69},
	number = {3},
	year = {1991},
	note = {ISI Document Delivery No.: FE808Times Cited: 18Cited Reference Count: 49},
	month = {Mar},
	pages = {391-396},
	type = {Article},
	abstract = {{Single crystals of gold(III) tris(fluorosulfate) are obtained by recrystallization from bis(fluorosulfuryl) peroxide, S2O6F2, under O2 pressure. The crystals of [Au(SO3F)3]2 are monoclinic},
	keywords = {CATIONS, CHEMISTRY, COMPLEXES, crystal structure, GOLD(III) FLUOROSULFATE, GOLD(III) TRIS(FLUOROSULFATE), HSO3F, ION, OXIDE, STABILITY},
	isbn = {0008-4042},
	url = {<Go to ISI>://A1991FE80800005},
	author = {Willner, H. and Rettig, S. J. and Trotter, J. and Aubke, F.}
}
@article {7148,
	title = {THE CRYSTAL AND MOLECULAR-STRUCTURE OF GOLD TRIS(FLUOROSULFATE)},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {69},
	number = {3},
	year = {1991},
	note = {ISI Document Delivery No.: FE808Times Cited: 18Cited Reference Count: 49},
	month = {Mar},
	pages = {391-396},
	type = {Article},
	abstract = {{Single crystals of gold(III) tris(fluorosulfate) are obtained by recrystallization from bis(fluorosulfuryl) peroxide, S2O6F2, under O2 pressure. The crystals of [Au(SO3F)3]2 are monoclinic},
	keywords = {CATIONS, CHEMISTRY, COMPLEXES, crystal structure, GOLD(III) FLUOROSULFATE, GOLD(III) TRIS(FLUOROSULFATE), HSO3F, ION, OXIDE, STABILITY},
	isbn = {0008-4042},
	url = {<Go to ISI>://A1991FE80800005},
	author = {Willner, H. and Rettig, S. J. and Trotter, J. and Aubke, F.}
}
