@article {2510,
	title = {The Engineering of Bacteria Bearing Azido-Pseudaminic Acid-Modified Flagella},
	journal = {Chembiochem},
	volume = {10},
	number = {8},
	year = {2009},
	note = {ISI Document Delivery No.: 452SMTimes Cited: 3Cited Reference Count: 24Liu, Feng Aubry, Annie J. Schoenhofen, Ian C. Logan, Susan M. Tanner, Martin E.},
	month = {May},
	pages = {1317-1320},
	type = {Article},
	keywords = {4, 6-DEHYDRATASE, azides, biosynthesis, C. jejuni, CAMPYLOBACTER-JEJUNI, cell surfaces, flagella, FUNCTIONAL-CHARACTERIZATION, HELICOBACTER-PYLORI, IDENTIFICATION, METABOLISM, PATHWAY, PROTEINS, PseB, reaction, Staudinger, UDP-N-ACETYLGLUCOSAMINE},
	isbn = {1439-4227},
	url = {<Go to ISI>://000266561500009},
	author = {Liu, F. and Aubry, A. J. and Schoenhofen, I. C. and Logan, S. M. and Tanner, M. E.}
}
@article {2415,
	title = {X-ray Crystal Analysis of a TASP: Structural Insights of a Cavitein Dimer},
	journal = {Journal of the American Chemical Society},
	volume = {131},
	number = {21},
	year = {2009},
	note = {ISI Document Delivery No.: 451QOTimes Cited: 0Cited Reference Count: 75Freeman, Jon O. Lee, Woo Cheol Murphy, Michael E. P. Sherman, John C.},
	month = {Jun},
	pages = {7421-7429},
	type = {Article},
	abstract = {Cavitein Q4 is a template assembled synthetic protein designed for X-ray crystallographic analysis. It is based on a previous monomeric helical bundle cavitein (N1GG) that consists of four identical parallel helical peptides. Crystals that were grown in the presence of bromide ions were used to solve the initial phases via single-wavelength anomalous dispersion (SAD). A 1.4 angstrom resolution data set was then refined starting with the SAD phases to provide the crystal structure of cavitein Q4. The crystal structure revealed cavitein Q4 as an asymmetric dimer, although the cavitein appears to be largely monomeric in solution. A comparative analysis is carried out to discern any intrinsic differences between Q4 and its parent cavitein N1GG. We present herein the first X-ray crystal structure of a TASP system and relate this structure to the solution data for both Q4 and its parent N1GG.},
	keywords = {4-HELIX BUNDLE, ALPHA-HELICES, ANALYTICAL, ANION-BINDING, ASSEMBLED SYNTHETIC PROTEINS, DE-NOVO PROTEINS, NATIVE-LIKE STRUCTURE, PEPTIDE-CAVITANDS, PROTEINS, SELF-ASSOCIATION, ULTRACENTRIFUGATION, UPPER RIM},
	isbn = {0002-7863},
	url = {<Go to ISI>://000266484900042},
	author = {Freeman, J. O. and Lee, W. C. and Murphy, M. E. P. and Sherman, J. C.}
}
@article {2342,
	title = {A novel functional polymer with tunable LCST},
	journal = {Macromolecules},
	volume = {41},
	number = {14},
	year = {2008},
	note = {ISI Document Delivery No.: 326NJTimes Cited: 13Cited Reference Count: 44Zou, Yuquan Brooks, Donald E. Kizhakkedathu, Jayachandran N.},
	month = {Jul},
	pages = {5393-5405},
	type = {Article},
	abstract = {Poly(N-[(2,2-dimethyl-1,3-dioxolane)methyl]acrylamide) (PDMDOMA), a novel thermo-responsive polymer containing pendant dioxolane groups was synthesized via atom transfer radical polymerization (ATRP). Water soluble PDMDOMAs with controlled molecular weight and narrow molecular weight distribution were obtained. GPC-MALLS and MALDI-TOF-MS analysis verified the controlled nature of polymerization. It was found that an aqueous solution of PDMDOMA has a lower critical solution temperature (LCST) around 23 degrees C. The LCST of PDMDOMA was finely tuned over a wide temperature range by the partial hydrolysis of the acid labile dioxolane side group to form diol moieties (PDMDOMA diols). Unlike the traditional way of controlling LCST by copolymerization, the advantage of this method is that a series of thermo-responsive polymers with different LCST can be prepared from a single batch of polymer with comparable molecular weight profiles. The LCST of the resulting PDMDOMA diols increased almost linearly up to 28 mol \% of diol in the copolymer and the LCST disappeared above 43 mol \% diol content. The diol moiety generated during the hydrolysis was further oxidized to create aldehyde functionalities along the polymer backbone (PDMDOMA-aldehyde). The NMR analysis indicates that the aldehyde groups in the polymer exist in equilibrium with their covalent hydrates in water. The presence and reactivity of aldehyde groups on the PDMDOMA-aldehyde was verified by reaction with propylamine and aniline. The LCST of PDMDOMA-aldehyde did not change significantly compared to the precursor diol polymer. However, the propylamine or aniline derivatives showed a dramatic decrease in the LSCT possibly due to an increase in the hydrophobic character. The LCST of PDMDOMA-propylamine and PDMDOMA-aniline derivatives depends on the composition and nature of the attached groups. The structure of PDMDOMA and its derivatives were fully characterized by H-1, C-13, and 2D HMQC NMR, GPC-MALLS, and MALDI-TOF-MS.},
	keywords = {2-(2-METHOXYETHOXY)ETHYL METHACRYLATE, AQUEOUS-SOLUTIONS, N-ISOPROPYLACRYLAMIDE, OLIGO(ETHYLENE GLYCOL) METHACRYLATE, POLYMERS, PROTEINS, SMART, SOLID TUMORS, STIMULI-RESPONSIVE POLYMERS, TEMPERATURE, TRANSFER RADICAL POLYMERIZATION},
	isbn = {0024-9297},
	url = {<Go to ISI>://000257665900045},
	author = {Zou, Y. Q. and Brooks, D. E. and Kizhakkedathu, J. N.}
}
@article {1545,
	title = {Characterization of de novo four-helix bundles by molecular dynamics simulations},
	journal = {Proteins-Structure Function and Bioinformatics},
	volume = {64},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 064QITimes Cited: 5Cited Reference Count: 34Scott, Walter R. P. Seo, Emily Huttunen, Heidi Wallhorn, Diana Sherman, John C. Straus, Suzana K.},
	month = {Aug},
	pages = {719-729},
	type = {Article},
	abstract = {We have investigated the structure and dynamics of three cavitand-based four-helix bundles (caviteins) by computer simulation. In these systems, designed de novo, each of the four helices contain the identical basis sequence EELLKKLEELLKKG (N1). Each cavitein consists of a rigid macrocycle (cavitand) with four aryl linkages, to each of which is connected an NI peptide by means of a linker peptide. The three caviteins studied here differ only in the linker peptide, which consist of one, two, or three glycine residues. Previous experimental work has shown that these systems exhibit very different behavior in terms of stability and oligomerization states despite the small differences in the linker peptide. Given that to date no three-dimensional structure is available for these caviteins, we have undertaken a series of molecular dynamics (MD) simulations in explicit water to try to rationalize the large differences in the experimentally observed behavior of these systems. Our results provide insight, for the first time, into why and how the cavitein with a single glycine linker forms dimers. In addition, our results indicate why although the two- and three-glycine-linked caviteins have similar stabilities, they have different native-like characteristics: the cavitein with three glycines can form a supercoiled helix, whereas the one with two glycines cannot. These findings may provide a useful guide in the rational de novo design of novel proteins with finely tunable structures and functions in the future.},
	keywords = {caviteins, de novo four-helix bundle, DESIGN, DOMAIN, HELICAL BUNDLES, molecular dynamics simulations, PEPTIDE, PROTEIN DESIGN, PROTEINS, STATE, SYSTEM, TASP, template-assembled synthetic protein},
	isbn = {0887-3585},
	url = {<Go to ISI>://000239103800014},
	author = {Scott, W. R. P. and Seo, E. and Huttunen, H. and Wallhorn, D. and Sherman, J. C. and Straus, S. K.}
}
@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 {1577,
	title = {Design of targeting ligands in medicinal inorganic chemistry},
	journal = {Chemical Society Reviews},
	volume = {35},
	number = {6},
	year = {2006},
	note = {ISI Document Delivery No.: 047UHTimes Cited: 58Cited Reference Count: 51},
	pages = {534-544},
	type = {Review},
	abstract = {This tutorial review will highlight recent advances in medicinal inorganic chemistry pertaining to the use of multifunctional ligands for enhanced effect. Ligands that adequately bind metal ions and also include specific targeting features are gaining in popularity due to their ability to enhance the efficacy of less complicated metal-based agents. Moving beyond the traditional view of ligands modifying reactivity, stabilizing specific oxidation states, and contributing to substitution inertness, we will discuss recent work involving metal complexes with multifunctional ligands that target specific tissues, membrane receptors, or endogenous molecules, including enzymes.},
	keywords = {CANCER, COMPLEXES, FLUORESCENCE, GADOLINIUM, IN-VITRO, PARACEST AGENTS, PROTEINS, RECEPTOR, therapy, TRANSPORT},
	isbn = {0306-0012},
	url = {<Go to ISI>://000237903700005},
	author = {Storr, T. and Thompson, K. H. and Orvig, Chris}
}
@article {1413,
	title = {Mass spectrometric characterization of lipid-modified peptides for the analysis of acylated proteins},
	journal = {Journal of Mass Spectrometry},
	volume = {41},
	number = {2},
	year = {2006},
	note = {ISI Document Delivery No.: 016BVTimes Cited: 13Cited Reference Count: 45},
	month = {Feb},
	pages = {229-241},
	type = {Article},
	abstract = {The analysis of acylated proteins by mass spectrometry (MS) has largely been overshadowed in proteomics by the analysis of glycosylated and phosphorylated proteins; however, lipid modifications on proteins are proving to be of increasing importance in biomedical research. In order to identify the marker ions and/or neutral loss fragments that are produced upon collision-induced dissociation, providing a means to identify the common lipid modifications on proteins, peptides containing an N-terminally myristoylated glycine, a palmitoylated cysteine and a farnesylated cysteine were chemically synthesized. Matrix-assisted laser desorption/ionization time-of-flight time-of-flight (MALDI-TOF-TOF), electrospray ionization quadrupole time-of-flight (ESI Q-TOF), and electrospray ionization hybrid triple-quadrupole/linear ion trap (ESI QqQ(LIT)) mass spectrometers were used for the analysis. The peptide containing the N-terminally myristoylated glycine, upon CID, produced the characteristic fragments a(1) (240.4 Th) and b(1) (268.4 Th) ions as well as a low-intensity neutral loss of 210 Da (C14H26O). The peptides containing a farnesylated cysteine residue fragmented to produce a marker ion at a m/z of 205 Th (C15H25) as well as other intense farnesyl fragment ions, and a neutral loss of 204 Da (C15H24). The peptides containing a palmitoylated cysteine moiety generated neutral losses of 238 Da (C16H30O) and 272 Da (C16H32OS); however, no marker ions were produced. The neutral losses were more prominent in the MALDI-TOF-TOF spectra, whereas the marker ions were more abundant in the ESI QqQ(LIT) and Q-TOF mass spectra. Copyright (c) 2006 John Wiley \& Sons, Ltd.},
	keywords = {ACID, ELECTROSPRAY-IONIZATION, farnesylation, IMMUNODEFICIENCY-VIRUS TYPE-1, marker ion, MATRIX PROTEIN, MEMBRANE ASSOCIATION, myristoylation, N-MYRISTOYLATION, neutral loss, palmitoylation, PHOSPHORYLATION, POSTTRANSLATIONAL MODIFICATIONS, PRENYLATED, PROTEINS},
	isbn = {1076-5174},
	url = {<Go to ISI>://000235596500011},
	author = {Hoffman, M. D. and Kast, J.}
}
@article {1484,
	title = {Molecular structure of fd (f1, M13) filamentous bacteriophage refined with respect to X-ray fibre diffraction and solid-state NMR data supports specific models of phage assembly at the bacterial membrane},
	journal = {Journal of Molecular Biology},
	volume = {355},
	number = {2},
	year = {2006},
	note = {ISI Document Delivery No.: 999EPTimes Cited: 30Cited Reference Count: 84},
	month = {Jan},
	pages = {294-309},
	type = {Article},
	abstract = {Filamentous bacteriophage (Inovirus) is a simple and well-characterized model system. The phage particle, or virion, is about 60 A in diameter and several thousand angstrom units long. The virions are assembled at the bacterial membrane as they extrude out of the host without killing it, an example of specific transport of nucleoprotein assemblages across membranes. The Ff group (fd, f1. and M13) has been especially widely studied. Models of virion assembly have been proposed based on a molecular model of the fd virion derived by X-ray fibre diffraction. A somewhat different model of the fd virion using solid-state NMR data has been proposed, not consistent with these models of assembly nor with the X-ray diffraction data. Here we show that reinterpreted NMR data are also consistent with the model derived from X-ray fibre diffraction studies, and discuss models of virion assembly. (c) 2005 Elsevier Ltd. All rights reserved.},
	keywords = {ALPHA-HELICES, ALPHA-HELIX, ATOMIC REFINEMENT, fibre diffraction, filamentous bacteriophage, INOVIRUS, MAJOR COAT PROTEIN, MEMBRANE, ORIENTATIONAL RESTRAINTS, PF1 BACTERIOPHAGE, PISEMA, PROTEINS, RESOLUTION, SINGLE-STRANDED-DNA, VIRION, VIRUS},
	isbn = {0022-2836},
	url = {<Go to ISI>://000234371900012},
	author = {Marvin, D. A. and Welsh, L. C. and Symmons, M. F. and Scott, W. R. P. and Straus, S. K.}
}
@article {1524,
	title = {Unambiguous determination of the ionization state of a glycoside hydrolase active site lysine by H-1-N-15 heteronuclear correlation spectroscopy},
	journal = {Journal of the American Chemical Society},
	volume = {128},
	number = {48},
	year = {2006},
	note = {ISI Document Delivery No.: 110GSTimes Cited: 15Cited Reference Count: 15Poon, David K. Y. Schubert, Mario Au, Jason Okon, Mark Withers, Stephen G. McIntosh, Lawrence P.},
	month = {Dec},
	pages = {15388-15389},
	type = {Article},
	keywords = {AMINO-ACIDS, beta, EXCHANGE, MAGNETIC-RESONANCE, NMR, PROTEINS},
	isbn = {0002-7863},
	url = {<Go to ISI>://000242367000018},
	author = {Poon, D. K. Y. and Schubert, M. and Au, J. and Okon, M. and Withers, S. G. and McIntosh, L. P.}
}
@article {959,
	title = {Efficient synthesis of isotopically pure isotope-coded affinity tagging reagents},
	journal = {Bioconjugate Chemistry},
	volume = {15},
	number = {1},
	year = {2004},
	note = {ISI Document Delivery No.: 766UDTimes Cited: 7Cited Reference Count: 24},
	month = {Jan-Feb},
	pages = {224-230},
	type = {Article},
	abstract = {Synthesis of an isotopically pure d(8)-ICAT linker, N- [(5,5,6,6,8,8 9,9-H-2)-13-biotinamido-4,7,10-trioxatridecanyl] tert-butyloxy carbamide (12), has been achieved in seven steps with an overall yield of 33\%. Conjugation of exchange-inert d(4)-starting materials by classic etherification reaction yielded a pure synthon, carrying eight deuteriums that remained exchange-inert throughout subsequent reactions. This modified synthesis constitutes a significant improvement to the reported syntheses of "heavy" ICAT reagent in terms of expense, yield, and isotopic retention. This synthesis is easily adapted to incorporate additional deuterium atoms and is equally applicable for incorporation of either C-13 and/or O-18. In addition, this synthesis allows for the introduction of different orthogonal functionalities and provides for a high yielding series of differentially encoded ICAT tags.},
	keywords = {GEL-ELECTROPHORESIS, IONIZATION MASS-SPECTROMETRY, LIQUID-CHROMATOGRAPHY, PEPTIDES, PROTEINS, PROTEOME ANALYSIS, TAGS},
	isbn = {1043-1802},
	url = {<Go to ISI>://000188393200027},
	author = {Patel, A. and Perrin,David M.}
}
@article {1015,
	title = {Triggering DNAzymes with light: A photoactive C8 thioether-linked adenosine},
	journal = {Journal of the American Chemical Society},
	volume = {126},
	number = {40},
	year = {2004},
	note = {ISI Document Delivery No.: 860QITimes Cited: 31Cited Reference Count: 36},
	month = {Oct},
	pages = {12720-12721},
	type = {Article},
	keywords = {BIOLOGICAL-ACTIVITY, DEOXYRIBOZYME, DNA, ENZYME, MESSENGER-RNA, NUCLEOSIDE, PROTEINS, PURINES},
	isbn = {0002-7863},
	url = {<Go to ISI>://000224357700005},
	author = {Ting, R. and Lermer, L. and Perrin,David M.}
}
@article {541,
	title = {Inhibitory module of Ets-1 allosterically regulates DNA binding through a dipole-facilitated phosphate contact},
	journal = {Journal of Biological Chemistry},
	volume = {277},
	number = {3},
	year = {2002},
	note = {ISI Document Delivery No.: 514CWTimes Cited: 21Cited Reference Count: 50},
	month = {Jan},
	pages = {2225-2233},
	type = {Article},
	abstract = {DNA binding of the transcription factor Ets-1 is negatively regulated by three inhibitory helices that lie near the ETS domain. The current model suggests that this negative regulation, termed autoinhibition, is caused by the energetic expense of a DNA-induced structural transition that includes the unfolding of one inhibitory helix. This report investigates the role of helix H1 of the ETS domain in the autoinhibition mechanism. Previous structural studies modeled the inhibitory helices packing together and connecting with helix H1, suggesting a role of this helix in the configuration of an inhibitory module. Recently, high-resolution structures of the ETS domain-DNA interface indicate that the N terminus of helix H1 directly contacts DNA. The contact, which is augmented by the macrodipole of helix H1, consists of a hydrogen bond between the amide NH of leucine 337 in helix HI and the oxygen of a corresponding phosphate. We propose that this hydrogen bond positions helix H1 to be a link between autoinhibition and DNA binding. Four independent approaches tested this hypothesis. First, the hydrogen bond was disrupted by removal of the phosphate in a missing phosphate analysis. Second, base pairs that surround the helix HI-contacting phosphate and appear to dictate DNA backbone conformation were mutated. Next, a hydrophobic residue in helix H1 that is expected to position the N terminus of the helix was altered. Finally, a residue on the surface of helix 111 that may contact the inhibitory elements was changed. In each case DNA binding and autoinhibition was affected. Taken together, the results demonstrate the role of the dipole-facilitated phosphate contact in DNA binding. Furthermore, the findings support a model in which helix H1 links the inhibitory elements to the ETS domain. We speculate that this helix, which is conserved in all Ets proteins, provides a common route to regulation.},
	keywords = {ALPHA-HELIX, AUTO-INHIBITION, COMPLEX, DOMAIN, FACTORS ELK-1, INDIRECT READOUT, MURINE ETS-1, PROTEINS, RECOGNITION, TRANSCRIPTION FACTOR},
	isbn = {0021-9258},
	url = {<Go to ISI>://000173421300083},
	author = {Wang, H. and McIntosh, L. P. and Graves, B. J.}
}
@article {438,
	title = {Letter to the Editor: Chemical shift and secondary structure conservation of the PNT/SAM domains from the Ets family of transcription factors},
	journal = {Journal of Biomolecular Nmr},
	volume = {24},
	number = {1},
	year = {2002},
	note = {ISI Document Delivery No.: 603GNTimes Cited: 6Cited Reference Count: 9},
	month = {Sep},
	pages = {71-72},
	type = {Letter},
	keywords = {Erg, Ets-1, GABP alpha, PNT domain, PROTEINS, SAM domain, secondary chemical shift, STEREOSPECIFIC ASSIGNMENT},
	isbn = {0925-2738},
	url = {<Go to ISI>://000178550700008},
	author = {Mackereth, C. D. and Scharpf, M. and Gentile, L. N. and McIntosh, L. P.}
}
@article {558,
	title = {An NMR approach to structural proteomics},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {99},
	number = {4},
	year = {2002},
	note = {ISI Document Delivery No.: 524UKTimes Cited: 109Cited Reference Count: 28},
	month = {Feb},
	pages = {1825-1830},
	type = {Article},
	abstract = {The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMIR. Although there was variability among proteomes, overall 20\% of these proteins were found to be readily amenable to NMR structure determination. NMIR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.},
	keywords = {ASSIGNMENTS, CATH, DOMAIN, PROGRAM, PROTEINS, SPECTRA},
	isbn = {0027-8424},
	url = {<Go to ISI>://000174031100016},
	author = {Yee, A. and Chang, X. Q. and Pineda-Lucena, A. and Wu, B. and Semesi, A. and Le, B. and Ramelot, T. and Lee, G. M. and Bhattacharyya, S. and Gutierrez, P. and Denisov, A. and Lee, C. H. and Cort, J. R. and Kozlov, G. and Liao, J. and Finak, G. and Chen, L. and Wishart, D. and Lee, W. and McIntosh, L. P. and Gehring, K. and Kennedy, M. A. and Edwards, A. M. and Arrowsmith, C. H.}
}
@article {4780,
	title = {Analysis of the dynamic properties of Bacillus circulans xylanase upon formation of a covalent glycosyl-enzyme intermediate},
	journal = {Protein Science},
	volume = {9},
	number = {3},
	year = {2000},
	note = {ISI Document Delivery No.: 295XWTimes Cited: 16Cited Reference Count: 56},
	month = {Mar},
	pages = {512-524},
	type = {Article},
	abstract = {NMR spectroscopy was used to search for mechanistically significant differences in the local mobility of the main-chain amides of Bacillus circulans xylanase (BCX) in its native and catalytically competent covalent glycosyl-enzyme intermediate states. N-15 T-1, T-2, and N-15{H-1} NOE values were measured for similar to 120 out of 178 peptide groups in both the apo form of the protein and in BCX covalently modified at position Glu78 with a mechanism-based 2-deoxy-2-fluoro-beta-xylobioside inactivator. Employing the model-free formalism of Lipari and Szabo, the measured relaxation parameters were used to calculate a global correlation time ( tau(m)) for the protein in each form (9.2 +/- 0.2 ns for apo-BCX; 9.8 +/- 0.3 ns for the modified protein), as well as individual order parameters for the main-chain NH bond vectors. Average values of the order parameters for the protein in the apo and complexed forms were S-2 = 0.86 +/- 0.04 and S-2 = 0.91 +/- 0.04, respectively. No correlation is observed between these order parameters and the secondary structure, solvent accessibility, or hydrogen bonding patterns of amides in either form of the protein. These results demonstrate that the backbone of BCX is well ordered in both states and that formation of the,glycosyl-enzyme intermediate leads to little change, in any, in the dynamic properties of BCX on the time scales sampled by N-15-NMR relaxation measurements.},
	keywords = {ACTIVE-SITE NUCLEOPHILE, ANISOTROPIC ROTATIONAL, BACKBONE DYNAMICS, BINDING, BURIED NEUTRAL HISTIDINE, DIFFUSION, glucanase, GLYCOSYL-ENZYME INTERMEDIATE, MAGNETIC-RESONANCE RELAXATION, MODEL-FREE APPROACH, N-15 NMR RELAXATION, NMR, order parameter, PROTEIN, PROTEINS, relaxation dynamics, SIDE-CHAIN RESONANCES, STRUCTURE},
	isbn = {0961-8368},
	url = {<Go to ISI>://000085994800009},
	author = {Connelly, G. P. and Withers, S. G. and McIntosh, L. P.}
}
@inbook {4963,
	title = {Cavitand templated de novo four-helix bundles},
	booktitle = {Peptides for the New Millennium},
	year = {2000},
	note = {ISI Document Delivery No.: BR58XTimes Cited: 0Cited Reference Count: 3Proceedings Paper16th American Peptide SymposiumJUN 26-JUL 01, 1999MINNEAPOLIS, MNAmer Peptide SocPO BOX 17, 3300 AA DORDRECHT, NETHERLANDS},
	pages = {295-296},
	publisher = {Springer},
	organization = {Springer},
	address = {Dordrecht},
	keywords = {PROTEINS},
	isbn = {0-7923-6445-7},
	url = {<Go to ISI>://000166856900119},
	author = {Wallhorn, D. and Mezo, A. R. and Sherman, J. C.},
	editor = {Fields, G. B. and Tam, J. P. and Barany, G.}
}
@article {4921,
	title = {Characterization of dissolved tannins and their metal-ion complexes by electrospray ionization mass spectrometry},
	journal = {Analytica Chimica Acta},
	volume = {411},
	number = {1-2},
	year = {2000},
	note = {ISI Document Delivery No.: 305EYTimes Cited: 25Cited Reference Count: 51},
	month = {May},
	pages = {91-102},
	type = {Article},
	abstract = {Electrospray mass spectrometry was used to characterize metal-complexing ligands derived from tannic acid, a component of natural dissolved organic matter. Complexes formed by tannin ligands with copper and other biogeochemically important metals were identified from the mass-to-charge ratios of the corresponding deprotonated molecular ions, allowing stoichiometry and metal oxidation state to be determined. Ligand ion intensities were proportional to tannic acid concentration, with detection limits on the order of 5 nM for individual compounds in 50:50 water/acetonitrile. The relative abundance of free ligand and complex ions indicated the degree of complexation under different solution conditions (metal concentration, pH, ionic strength). Using tandem mass spectrometry, the structure and principal copper binding site for one of the tannins were also determined, providing unique information with regard to metal complexation by these polyfunctional ligands. The technique can be combined with high performance liquid chromatography for on-line separation of dissolved organic compounds. Results demonstrate the potential of this approach for characterizing the different classes of metal-complexing ligands found in natural waters. (C) 2000 Elsevier Science B.V. All rights reserved.},
	keywords = {AFFINITY-CHROMATOGRAPHY, CHROMATOGRAPHY, COMPLEXATION, copper, electrospray ionization, high performance liquid, iron, LIGANDS, MASS SPECTROMETRY, metal-ion complexes, NATURAL ORGANIC-LIGANDS, ORGANIC, PERFORMANCE, PROTEINS, REGIOSELECTIVE MONO-OXIDATION, SPECIATION, STOICHIOMETRY, tannins, TOXICITY, trace metals},
	isbn = {0003-2670},
	url = {<Go to ISI>://000086527500011},
	author = {Ross, A. R. S. and Ikonomou, M. G. and Orians, K. J.}
}
@article {4924,
	title = {Collision-induced dissociation of ions within the orifice-skimmer region of an electrospray mass spectrometer},
	journal = {Analytical Chemistry},
	volume = {72},
	number = {4},
	year = {2000},
	note = {ISI Document Delivery No.: 285HETimes Cited: 38Cited Reference Count: 33},
	month = {Feb},
	pages = {791-799},
	type = {Article},
	abstract = {An equation was derived to describe the variation of the gas number density within the region between the orifice and the skimmer of an electrospray ionization mass spectrometer. The equation was used to develop a semiquantitative model to predict the value of orifice voltages that lead to ion fragmentation within this region. This model made it possible to predict the types of solvent adducts observed for analytes at various orifice voltages. In addition, it is shown that a small number of high-energy collisions is equally effective for collision-induced dissociation as compared to a large number of low-energy collisions. Finally, this model is tested with different background electrolyte solutions and a different electrospray mass spectrometer. It is demonstrated that controlled fragmentation studies can be performed on single-quadrupole mass spectrometers, and the proposed model gives a reasonable description of the fragmentation process in both spectrometers.},
	keywords = {capillary electrophoresis, CYTOCHROME-C, DYNAMICS, IDENTIFICATION, INTERFACE, IONIZATION, LIQUID-CHROMATOGRAPHY, PROTEINS, SENSITIVITY, SEPARATION},
	isbn = {0003-2700},
	url = {<Go to ISI>://000085383000019},
	author = {Schneider, B. B. and Chen, D. D. Y.}
}
@article {4920,
	title = {Electrospray ionization of alkali and alkaline earth metal species. Electrochemical oxidation and pH effects},
	journal = {Journal of Mass Spectrometry},
	volume = {35},
	number = {8},
	year = {2000},
	note = {ISI Document Delivery No.: 347MUTimes Cited: 7Cited Reference Count: 49},
	month = {Aug},
	pages = {981-989},
	type = {Article},
	abstract = {The utility of electrospray ionization mass spectrometry (ESI-MS) for characterizing dissolved metal species has generated considerable interest in the use of this technique for metal speciation, However, the development of accurate speciation methods based on ESI-R;IS requires a detailed understanding of the mechanisms by which dissolved metal species are ionized during electrospray. We report how the analysis of alkali and alkaline earth metal species pro,ides new information about some of the processes that affect electrospray ion yield. Selected metal ions and organic ligands were combined in 50:50 water-acetonitrile buffered with acetic acid or ammonium acetate and analyzed by flow injection ESI-MS using mild electrospray conditions. Species formed by alkali metal ions with thiol and oxygen-donating ligands were detected in acidic and neutral pH solutions. Electrochemical oxidation of N,N-diethyldithiocarbamate and glutathione during electrospray was indicated by detection of the corresponding disulfides as protonated or alkali metal species, The extent of ligand oxidation depended on solution pH and the dissociation constant of the thiol group, Tandem mass spectrometric experiments suggested that radical cations such as [NaL](+.) (where L = N,N -diethyldithiocarbamate) can be generated by in-source fragmentation of disulfide species. Greater complexation of alkali metals at neutral pH tvas indicated by a corresponding decrease in the relative abundance of the free metal ion, The number of alkali metal ions bound by glutathione and phthalic acid also increased with increasing pH, in accordance with thermodynamic equilibrium theory. Alkaline earth metal species were detected only in acidic solutions, the absence of 8-hydroxyquinoline complexes being attributed to their relative instability and subsequent dissociation during electrospray, Hence, accurate speciation by ESI-MS depends on experimental conditions and the intrinsic properties of each analyte, Copyright (C) 2000 John Wiley \&; Sons, Ltd.},
	keywords = {cell, COMPLEXES, electrochemical oxidation, ELECTROPHORESIS, electrospray ionization, ION-TRAP, MASS-SPECTROMETRY, metal speciation, OLIGONUCLEOTIDES, PEPTIDES, pH effects, PROTEINS, STOICHIOMETRY, thiol ligands, WATER},
	isbn = {1076-5174},
	url = {<Go to ISI>://000088934400006},
	author = {Ross, A. R. S. and Ikonomou, M. G. and Orians, K. J.}
}
@article {4753,
	title = {An interface with a linear quadrupole ion guide for an electrospray-ion trap mass spectrometer system},
	journal = {Analytical Chemistry},
	volume = {72},
	number = {22},
	year = {2000},
	note = {ISI Document Delivery No.: 374LNTimes Cited: 30Cited Reference Count: 41},
	month = {Nov},
	pages = {5647-5654},
	type = {Article},
	abstract = {A new ion sampling interface for an electrospray ionization 3D ion trap mass spectrometer system is described. The interface uses linear rf quadrupoles as ion guides and ion traps to enhance the performance of the 3D trap. Trapping ions in the linear quadrupoles is demonstrated to improve the duty cycle of the system. Dipolar excitation of ions trapped in a linear quadrupole is used to eject unwanted ions, A resolution of ejection of up to 254 is demonstrated for protonated reserpine ions (m/z 609.3), A composite waveform with a notch in frequency space is used to eject a wide range of matrix ions and to isolate trace analyte ions in a linear quadrupole before ions are injected into the 3D trap. This is useful to overcome space charge problems in the 3D trap caused by excess matrix ions. For trace reserpine in a 500-fold molar excess of poly(propylene glycol) (PPG), it is demonstrated that the resolution and sensitivity of the 3D trap can be increased dramatically with ejection of the excess PPG matrix ions. In comparison to ejection of matrix ions in the 3D trap with a similar broad-band waveform, a ii-fold increase in sensitivity with a 7 times shorter acquisition time was achieved.},
	keywords = {accumulation, ACCURACY, DIGESTS, DISSOCIATION, FILTERED NOISE FIELD, INJECTION, IONIZATION, PEPTIDES, PROTEINS, storage},
	isbn = {0003-2700},
	url = {<Go to ISI>://000165346800018},
	author = {Cha, B. C. and Blades, M. W. and Douglas, D. J.}
}
@inbook {4841,
	title = {Macromolecular crowding and its consequences},
	booktitle = {International Review of Cytology - a Survey of Cell Biology, Vol 192},
	series = {International Review of Cytology-a Survey of Cell Biology},
	volume = {192},
	year = {2000},
	note = {ISI Document Delivery No.: BP32STimes Cited: 19Cited Reference Count: 30Review525 B STREET, SUITE 1900, SAN DIEGO, CA 92101-4495 USA},
	pages = {155-170},
	publisher = {Academic Press Inc},
	organization = {Academic Press Inc},
	address = {San Diego},
	keywords = {AQUEOUS-SOLUTIONS, CYTOPLASM, DIAGRAMS, Flory-Huggins theory, incompatibilty, PHASE, PHASE-SEPARATION, PROTEINS, scaled particle theory, THERMODYNAMIC INCOMPATIBILITY},
	isbn = {0074-7696},
	url = {<Go to ISI>://000084720600006},
	author = {Johansson, H. O. and Brooks, D. E. and Haynes, C. A.}
}
@article {4873,
	title = {Zinc-bundle structure of the essential RNA polymerase subunit RPB10 from Methanobacterium thermoautotrophicum},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {97},
	number = {12},
	year = {2000},
	note = {ISI Document Delivery No.: 322UATimes Cited: 14Cited Reference Count: 34},
	month = {Jun},
	pages = {6316-6321},
	type = {Article},
	abstract = {The RNA polymerase subunit RPB10 displays a high level of conservation across archaea and eukarya and is required for cell viability in yeast, Structure determination of this RNA polymerase subunit from Methanobacterium thermoautotrophicum reveals a topology, which we term a zinc-bundle, consisting of three cu-helices stabilized by a zinc ion. The metal ion is bound within an atypical CX2CXnCC sequence motif and serves to bridge an N-terminal loop with helix 3, This represents an example of two adjacent zinc-binding Cys residues within an alpha-helix conformation. Conserved surface features of RPB10 include discrete regions of neutral, acidic, and basic residues, the latter being located around the zinc-binding site. One or more of these regions may contribute to the role of this subunit as a scaffold protein within the polymerase holoenzyme.},
	keywords = {ABC10-BETA, ARCHAEA, COMMON SUBUNITS, DOMAIN, genomics, IN-VITRO, PROTEINS, RESOLUTION, SEQUENCE, transcription},
	isbn = {0027-8424},
	url = {<Go to ISI>://000087526300018},
	author = {Mackereth, C. D. and Arrowsmith, C. H. and Edwards, A. M. and McIntosh, L. P.}
}
@article {4661,
	title = {Cationic iron(III) complex with a hexadentate N-2,N {\textquoteright}(2),O-2-aminopyridylphenolate ligand},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {77},
	number = {12},
	year = {1999},
	note = {ISI Document Delivery No.: 262KYTimes Cited: 14Cited Reference Count: 34},
	month = {Dec},
	pages = {2033-2038},
	type = {Article},
	abstract = {{Iron(III) complexation with potentially hexadentate H(2)bbpen (N,N{\textquoteright}-bis(2-hydroxybenzyl)-N,N{\textquoteright}-bis(2-methylpyridyl)ethylenediamine) was studied. The resulting monocationic complex, [Fe(bbpen)](+) as its NO3- and PF6- salts, was characterized by infrared spectroscopy, mass spectrometry, elemental analyses, cyclic voltammetry, and X-ray crystallographic analysis. Crystals of [Fe(bbpen)]NO3. CH3OH are monoclinic, space group P2(1)/c},
	keywords = {ANALOGS, BINDING-SITE, CATIONIC, CRYSTAL-STRUCTURE, gallium, hexadentate, indium, iron( III), LACTOFERRIN, MODEL, OXO, phenolate, PROTEINS, pyridyl},
	isbn = {0008-4042},
	url = {<Go to ISI>://000084067500004},
	author = {Setyawati, I. A. and Rettig, S. J. and Orvig, Chris}
}
@article {4578,
	title = {The cellulose-binding domains from Cellulomonas fimi beta-1,4-glucanase CenC bind nitroxide spin-labeled cellooligosaccharides in multiple orientations},
	journal = {Journal of Molecular Biology},
	volume = {287},
	number = {3},
	year = {1999},
	note = {ISI Document Delivery No.: 184RGTimes Cited: 38Cited Reference Count: 46},
	month = {Apr},
	pages = {609-625},
	type = {Article},
	abstract = {The N-terminal cellulose-binding domains CBDN1 and CBDN2 from Cellulomonas fimi cellulase CenC each adopt a jelly-roll beta-sandwich structure with a cleft into which amorphous cellulose and soluble cellooligosaccharides bind. To determine the orientation of the sugar chain within these binding clefts, the association of TEMPO (2,2,6,6-tetramethylpiperidine-1-oxyl-4-yl) spin-labeled derivatives of cellotriose and cellotetraose with isolated CBDN1 and CBDN2 was studied using heteronuclear H-1-N-15 NMR spectroscopy. Quantitative binding measurements indicate that the TEMPO moiety does not significantly perturb the affinity of the cellooligo-saccharide derivatives for the CBDs. The paramagnetic enhancements of the amide H-1(N) longitudinal (Delta R-1) and transverse (Delta R-2) relaxation rates were measured by comparing the effects of TEMPO-cellotetraose in its nitroxide (oxidized) and hydroxylamine (reduced) forms on the two CBDs. The bound spin-label affects most significantly the relaxation rates of amides located at both ends of the sugar-binding cleft of each CBD. Similar results are observed with TEMPO-cellotriose bound to CBDN1. This demonstrates that the TEMPO-labeled cellooligosaccharides, and by inference strands of amorphous cellulose, can associate with CBDN1 and CBDN2 in either orientation across their beta-sheet binding clefts. The ratio of the association constants for binding in each of these two orientations is estimated to be within a factor of five to tenfold. This finding is consistent with the approximate symmetry of the hydrogen-bonding groups on both the cellooligosaccharides and the residues forming the binding clefts of the CenC CBDs. (C) 1999 Academic Press.},
	keywords = {CELLULASES, ENDOGLUCANASE, GLYCOSYNTHASE, MAGNETIC-RESONANCE SPECTROSCOPY, NMR, protein-carbohydrate interaction, PROTEINS, SENSITIVITY, SITE, SPECIFICITY, spin label},
	isbn = {0022-2836},
	url = {<Go to ISI>://000079626300013},
	author = {Johnson, P. E. and Brun, E. and Mackenzie, L. F. and Withers, S. G. and McIntosh, L. P.}
}
@article {4486,
	title = {Clq binding to liposomes is surface charge dependent and is inhibited by peptides consisting of residues 14-26 of the human ClqA chain in a sequence independent manner},
	journal = {Biochimica Et Biophysica Acta-Biomembranes},
	volume = {1418},
	number = {1},
	year = {1999},
	note = {ISI Document Delivery No.: 189EWTimes Cited: 20Cited Reference Count: 36},
	month = {Apr},
	pages = {19-30},
	type = {Article},
	abstract = {Complement activation by anionic liposomes proceeds by antibody-independent, C1q-initiated activation of the classical pathway. Purified C1q bound to anionic liposomes in an acidic lipid concentration-dependent manner. Saturation binding, but not the apparent association constant, was enhanced by increasing the cardiolipin content of the liposomes or decreasing either the pH or ionic strength of the reaction mixture. These observations indicate the involvement of electrostatic factors in the binding. A highly cationic region in the collagen-like domain of C1q comprised of residues 14-26 of the C1qA polypeptide chain was assessed for involvement in liposome binding. This region has previously been shown to mediate C1q binding to other immunoglobulin-independent activators of the classical pathway of complement. Peptides containing residues 14-26 of C1qA, denoted C1qA(14-26), inhibited C1q binding to and complement activation by anionic liposomes. The inhibitory capacity of these cationic peptides had no sequence or conformation specificity. Rather, the amount of positive charge on the peptides was the determining factor. When present in excess, peptides with five cationic residues inhibited C1q binding and complement activation; however, C1q peptides with only two cationic residues did not. In addition to the C1qA(14-26) region, other parts of C1q that contain cationic residues may also be involved in C1q binding to anionic liposomes. (C) 1999 Elsevier Science B.V. All rights reserved.},
	keywords = {1ST, ACTIVATES COMPLEMENT, C1Q A-CHAIN, CLASSICAL COMPLEMENT PATHWAY, CLEARANCE, Clq binding, COLLAGEN, COMPONENT, liposome clearance, liposome-mediated complement activation, PHAGOCYTOSIS, PROTEINS, SERUM, SYSTEM},
	isbn = {0005-2736},
	url = {<Go to ISI>://000079892300002},
	author = {Bradley, A. J. and Brooks, D. E. and Norris-Jones, R. and Devine, D. V.}
}
@article {4554,
	title = {Computational prediction of the enantioselectivity of a solid-state photoreaction},
	journal = {Organic Letters},
	volume = {1},
	number = {8},
	year = {1999},
	note = {ISI Document Delivery No.: 281QKTimes Cited: 8Cited Reference Count: 26},
	month = {Oct},
	pages = {1279-1281},
	type = {Article},
	abstract = {[GRAPHICS] To better understand the forces controlling chemical reactions in crystals, the absolute asymmetric photorearrangement of 4-m-chlorobenzyloxy-2-pyridone leading to the corresponding enantiomerically enriched (78\% ee) beta-lactam was modeled computationally using a flexible minilattice consisting of a central reactant and 20 nearest and 72 next-nearest neighbors. The computational results predicted a preference for formation of the (R,R)-enantiomer, and this was verified experimentally by absolute configuration correlation studies.},
	keywords = {ABSOLUTE ASYMMETRIC-SYNTHESIS, CRYSTAL LATTICES, FORCE-FIELD, MEDIA, MODEL, MOLECULAR MECHANICS, NUCLEIC-ACIDS, PHOTOCHEMISTRY, PROTEINS},
	isbn = {1523-7060},
	url = {<Go to ISI>://000085172100037},
	author = {Garcia-Garibay, M. A. and Houk, K. N. and Keating, A. E. and Cheer, C. J. and Leibovitch, M. and Scheffer, J. R. and Wu, L. C.}
}
@article {4235,
	title = {Characterization of a buried neutral histidine in Bacillus circulans xylanase: Internal dynamics and interaction with a bound water molecule},
	journal = {Biochemistry},
	volume = {37},
	number = {7},
	year = {1998},
	note = {ISI Document Delivery No.: YZ886Times Cited: 13Cited Reference Count: 59},
	month = {Feb},
	pages = {1810-1818},
	type = {Article},
	abstract = {NMR spectroscopy was used to characterize the dynamic behavior of His149 in Bacillus circulans xylanase (BCX) and its interaction with an internal water molecule. Rate constants for the specific acid-and base-catalyzed exchange following bimolecular kinetics (EX2) of the nitrogen-bonded H-epsilon 2 of this buried, neutral histidine were determined, At pD(min) 7.0 and 30 degrees C, the lifetime for this proton is 9.9 h, corresponding to a protection factor of similar to 10(7) relative to that predicted for an exposed histidine, The apparent activation energies measured for specific acid and base catalysis (7.0 and 17.4 kcal/mol) indicate that exchange occurs via local structural fluctuations. Consistent with its buried environment, the N-epsilon 2-H bond vector of His149 shows restricted mobility, as evidenced by an order parameter S-2 = 0.83 determined from N-15 relaxation measurements, The crystal structure of BCX reveals that a conserved, buried water hydrogen-bonds to the H-epsilon 2 of His149. Strong support for this interaction in solution is provided by the observation of a negative nuclear Overhauser effect (NOE) and positive rotating-frame Overhauser effect (ROE) between His149 H-epsilon 2 and a water molecule with the same chemical shift as the bulk solvent. However, the chemical shift of H-epsilon 2 (12.2 ppm) and a D/H fractionation factor close to unity (0.89 +/- 0.02) indicate that this is nor a so-called low-barrier hydrogen bond. Lower and upper bounds on the lifetime of the internal water are estimated to be 10(-8) and 10(-3) s. Therefore the chemical exchange of solvent protons with those of His149 H-epsilon 2 and the diffusion or physical exchange of the internal water to which the histidine is hydrogen-bonded differ in rate by over 7 orders of magnitude.},
	keywords = {ACTIVE-SITE, AMIDE PROTON-EXCHANGE, ASSIGNMENTS, DOMAIN, HYDROGEN-BOND, NMR-SPECTROSCOPY, NUCLEAR MAGNETIC-RESONANCE, PROTEINS, relaxation, TRICHODERMA-REESEI},
	isbn = {0006-2960},
	url = {<Go to ISI>://000072304200010},
	author = {Connelly, G. P. and McIntosh, L. P.}
}
@article {4394,
	title = {Determination of dissolved metal species by electrospray ionization mass spectrometry},
	journal = {Analytical Chemistry},
	volume = {70},
	number = {11},
	year = {1998},
	note = {ISI Document Delivery No.: ZR483Times Cited: 49Cited Reference Count: 50},
	month = {Jun},
	pages = {2225-2235},
	type = {Article},
	abstract = {The distribution of metal species in solution was determined using now injection electrospray ionization mass spectrometry. Complexes formed by selected metal ions with added organic ligands in 50:50 water/acetonitrile and 50:50 water/methanol under acidic, neutral, and basic conditions were detected using electrospray ionization conditions optimized to best represent solution-phase interactions. Metal species containing acetate, nitrate, and solvent molecules predominated in acidic solution but became less abundant at higher pH. Interactions between metal ions and added organic ligands became more selective with increasing pH, showing the expected preference of hard and soft ligands for metal ions:of the corresponding type. Species distributions also tended toward larger complexes as pH increased. Overall ion yield was greater for aqueous acetonitrile than for aqueous methanol solutions; however, reduction of copper(II) in aqueous acetonitrile resulted in the detection of copper(I) complexes for certain ligands. Experimental results for copper(II) and 8-hydroxyquinoline in 50:50 water/methanol showed good agreement with aqueous speciation predicted using the thermodynamic equilibrium model MINEQL. Detection of neutral complexes was achieved by protonation, deprotonation, or electrochemical oxidation during electrospray.},
	keywords = {COMPLEXES, copper, GAS-PHASE, LIGANDS, PHASE ION CHEMISTRY, PROTEINS, SOLVENT, SPECIATION, STOICHIOMETRY},
	isbn = {0003-2700},
	url = {<Go to ISI>://000073981600011},
	author = {Ross, A. R. S. and Ikonomou, M. G. and Thompson, J. A. J. and Orians, K. J.}
}
@article {4222,
	title = {A new linear ion trap time-of-flight system with tandem mass spectrometry capabilities},
	journal = {Rapid Communications in Mass Spectrometry},
	volume = {12},
	number = {20},
	year = {1998},
	note = {ISI Document Delivery No.: 130DBTimes Cited: 92Cited Reference Count: 64},
	pages = {1463-1474},
	type = {Article},
	abstract = {A new hybrid linear ion trap time-of-flight mass spectrometer has been constructed and the first results for tandem-in-time MS/MS in a 2-dimensional Paul trap are presented. The instrument consists of an electrospray ionization source and two radio frequency (RF) only quadrupoles operating at a pressure of 7 mTorr N-2 which are coupled orthogonally to a linear TOFMS. Ions are trapped in an RF-only quadrupole through the application of timed stopping potentials on the entrance and exit apertures. Through the coupling of an auxiliary waveform generator on one pair of the ion trap rods a small dipolar excitation voltage is superimposed on the quadrupolar electric field. This voltage is used for precursor isolation via broadband excitation and collision induced dissociation through mass selective resonant excitation. Instrumental performance and choice of operating parameters are demonstrated by recording fragment spectra for +3 ions of renin substrate and fl ions of reserpine. TOFMS mass resolution (m/Delta m)(FWHM) is as high as 740 at m/z = 609. Fragmentation efficiency is greater than 50\% and excitation mass resolution is 60-75. (C) 1998 John Wiley \& Sons, Ltd.},
	keywords = {DECOMPOSITION, EJECTION, ELECTROSPRAY-IONIZATION, FREQUENCY STANDARD APPLICATIONS, MOLECULE REACTION, PARAMETERS, PERFORMANCE, PROTEINS, QUADRUPOLE, RESONANCE, SPECTROSCOPY},
	isbn = {0951-4198},
	url = {<Go to ISI>://000076503200007},
	author = {Campbell, J. M. and Collings, B. A. and Douglas, D. J.}
}
@article {4166,
	title = {Bidentate sulfoxide complexes of ruthenium(II) and their preliminary biological assessment in vitro},
	journal = {Inorganic Chemistry},
	volume = {36},
	number = {24},
	year = {1997},
	note = {ISI Document Delivery No.: YH560Times Cited: 22Cited Reference Count: 57},
	month = {Nov},
	pages = {5635-5641},
	type = {Article},
	abstract = {{The complexes trans-RuCl2(BMSE)(2) (1), cis-RuCl2(BESE)(2) (2), trans-RuCl2(BPSE)(2) (3), and cis-RuCl2(BMSP)(2) (4) have been synthesized and characterized, including X-ray analyses [BMSE = 1,2-bis(methylsulfinyl)ethane},
	keywords = {CISPLATIN-DAMAGED DNA, HAMSTER OVARY CELLS, LIGANDS, nuclear, PROTEINS, RADIOSENSITIZING ACTIVITY, REACTION-PRODUCT, SOLUTION CHEMISTRY, STRUCTURAL CHARACTERIZATION, SULFOXIDE)RUTHENIUM(II), TRANS-RUCL2(DMSO)4},
	isbn = {0020-1669},
	url = {<Go to ISI>://A1997YH56000034},
	author = {Yapp, D. T. T. and Rettig, S. J. and James, Brian R. and Skov, K. A.}
}
@article {4020,
	title = {Complete measurement of the pK(a) values of the carboxyl and imidazole groups in Bacillus circulans xylanase},
	journal = {Protein Science},
	volume = {6},
	number = {12},
	year = {1997},
	note = {ISI Document Delivery No.: YK912Times Cited: 44Cited Reference Count: 29},
	month = {Dec},
	pages = {2667-2670},
	type = {Article},
	abstract = {Electrostatic interactions in proteins can be dissected experimentally by determining the pK(a), values of their constituent ionizable amino acids. To complement previous studies of the glutamic acid and histidine residues in Bacillus circulans xylanase (BCX), we have used NMR methods to measure the pK(a)s of the seven aspartic acids and the C-terminus of this protein. The pK(a)s of these carboxyls are all less than the corresponding values observed with random coil polypeptides, indicating that their ionization contributes favorably to the stability of the folded enzyme. In general, the aspartic acids with the most reduced pK(a)s are those with limited exposure to the solvent and a high degree of conservation among homologous xylanases. Most dramatically, Asp 53 and Asp 101 have pK(a)s < 2 and thus remain deprotonated in native BCX under all conditions examined. Asp 83 is completely buried, forming a strong salt bridge with Arg 136. In contrast, Asp 101 is located on the surface of the protein, stabilized in the deprotonated form by an extensive network of hydrogen bonds involving an internal water molecule and the neutral side-chain and main-chain atoms of Ser 100 and Thr 145. These data provide a complete experimental database for theoretical studies of the ionization behavior of BCX under acidic conditions.},
	keywords = {aspartic acid, electrostatics, FAMILIES, NMR, NMR ASSIGNMENTS, NUCLEAR-MAGNETIC-RESONANCE, PK(A), PROTEINS, RESIDUES, SHIFTS, titration, XYLANASE},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1997YK91200024},
	author = {Joshi, M. D. and Hedberg, A. and McIntosh, L. P.}
}
@article {4028,
	title = {Cytochrome c folding kinetics studied by time-resolved electrospray ionization mass spectrometry},
	journal = {Biochemistry},
	volume = {36},
	number = {18},
	year = {1997},
	note = {ISI Document Delivery No.: WY063Times Cited: 82Cited Reference Count: 46},
	month = {May},
	pages = {5554-5559},
	type = {Article},
	abstract = {A new method for studying the folding kinetics of proteins is described. The method combines a continuous flow mixing technique with an electrospray mass spectrometer. Different protein conformations in solution are detected by the different charge states they produce during electrospray ionization. Unfolded proteins generally have more accessible protonation sites and give higher charge states than native proteins. The method is applied to study the refolding of acid-denatured cytochrome c. Global data analysis is used to obtain the exponential lifetimes which are associated with the refolding process. The kinetics can be described by two lifetimes of 0.17 +/- 0.02 and 8.1 +/- 0.9 s which are in accordance with the results of stopped flow experiments previously described in the literature. These lifetimes are associated with roughly 90 and 10\% of the total intensity changes in the mass spectrum, respectively, and most likely reflect fast and slow refolding subpopulations of cytochrome c in solution.},
	keywords = {COMPLEX, denaturation, FERRICYTOCHROME-C, IRON BLEOMYCIN, LIGANDS, MECHANISM, PATHWAYS, PROBING CONFORMATIONAL-CHANGES, PROTEINS, SPECTRA},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1997WY06300029},
	author = {Konermann, L. and Collings, B. A. 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.}
}
@article {3984,
	title = {On-line monitoring and control of methanol concentration in shake-flask cultures of Pichia pastoris},
	journal = {Biotechnology and Bioengineering},
	volume = {56},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: XZ728Times Cited: 48Cited Reference Count: 19},
	month = {Nov},
	pages = {279-286},
	type = {Article},
	abstract = {The methylotrophic yeast Pichia pastoris can be used to express recombinant genes at high levels under the control of the methanol-inducible alcohol oxidase 1 (AOX1) promoter. Accurate regulation of the methanol concentration in P. pastoris cultures is necessary to maintain induction, while preventing accumulation of methanol to cytotoxic levels. We developed an inexpensive methanol sensor that uses a gas-permeable silicone rubber tube immersed in the culture medium and an organic solvent vapor detector. The sensor was used to monitor methanol concentration continuously throughout a fed-batch shake-flask culture of a P. pastoris clone producing the N-lobe of human transferrin. The sensor calibration was stable for the duration of the culture and the output signal accurately reflected the methanol concentration determined off-line by HPLC. A closed-loop control system utilizing this sensor was developed and used to maintain a 0.3\% (v/v) methanol concentration in the culture. Use of this system resulted in a fivefold increase in volumetric protein productivity over levels obtained using the conventional fed-batch protocol. (C) 1997 John Wiley \& Sons, Inc.},
	keywords = {fermentation, GENE-EXPRESSION, methanol monitoring and control, methanol sensor, methylotrophic yeast, Pichia pastoris, PROTEINS, SEMICONDUCTOR GAS SENSORS, shake-flask cultures, TRANSFERRIN, YEAST},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1997XZ72800005},
	author = {Guarna, M. M. and Lesnicki, G. J. and Tam, B. M. and Robinson, J. and Radziminski, C. Z. and Hasenwinkle, D. and Boraston, A. and Jervis, E. and MacGillivray, R. T. A. and Turner, R. F. B. and Kilburn, D. G.}
}
@article {3635,
	title = {Conformation of gas-phase myoglobin ions},
	journal = {Journal of the American Chemical Society},
	volume = {118},
	number = {18},
	year = {1996},
	note = {ISI Document Delivery No.: UK145Times Cited: 89Cited Reference Count: 33},
	month = {May},
	pages = {4488-4489},
	type = {Article},
	keywords = {CYTOCHROME-C, ELECTROSPRAY MASS-SPECTROMETRY, IONIZATION, PROTEINS},
	isbn = {0002-7863},
	url = {<Go to ISI>://A1996UK14500034},
	author = {Collings, B. A. and Douglas, D. J.}
}
@article {3762,
	title = {The pK(a) of the general acid/base carboxyl group of a glycosidase cycles during catalysis: A C-13-NMR study of Bacillus circuluns xylanase},
	journal = {Biochemistry},
	volume = {35},
	number = {31},
	year = {1996},
	note = {ISI Document Delivery No.: VB211Times Cited: 149Cited Reference Count: 43},
	month = {Aug},
	pages = {9958-9966},
	type = {Article},
	abstract = {The 20 kDa xylanase from Bacillus circulans carries out hydrolysis of xylan via a two-step mechanism involving a covalent glycosyl-enzyme intermediate. In this double-displacement reaction, Glu78 functions as a nucleophile to form the intermediate, while Glu172 acts as a general acid catalyst during glycosylation, protonating the departing aglycone, and then as a general base during deglycosylation, deprotonating the attacking water, The dual role of Glu172 places specific demands upon its ionization states and hence pK(a) values. C-13-NMR titrations of xylanase, labeled with [delta-C-13]glutamic acid, have revealed pK(a) values of 4.6 and 6.7 for Glu78 and Glu172, respectively. These agree well with the apparent pK(a) values obtained from a study of the pH dependence of k(cat)/K-m and demonstrate that, at the enzyme{\textquoteright}s pH optimum of 5.7, the nucleophile Glu78 is deprotonated and the general acid Glu172 initially protonated. Remarkably, the pK(a) for Glu172 drops to 4.2 in a trapped covalent glycosyl-enzyme intermediate, formed by reaction with 2{\textquoteright},4{\textquoteright}-dinitrophenyl 2-deoxy-2-fluoro-beta-xylobioside [Miao et al. (1994) Biochemistry 33, 7027-7032], A similar pK(a) is measured for Glu172 when a glutamine is present at position 78. This large decrease in pK(a) of similar to 2.5 units is consistent with the role of Glu172 as a general base catalyst in the deglycosylation step and appears to be a consequence of both reduced electrostatic repulsion due to neutralization of Glu78 and a conformational change in the protein. Such {\textquoteright}{\textquoteright}pK(a) cycling{\textquoteright}{\textquoteright} during catalysis is likely to be a common phenomenon in glycosidases.},
	keywords = {ACTIVE-SITE RESIDUES, AMINO-ACIDS, beta-glucosidase, ELECTROSTATIC INTERACTIONS, ESCHERICHIA-COLI, IDENTIFICATION, LYSOZYME, MECHANISMS, NUCLEAR-MAGNETIC-RESONANCE, PROTEINS},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1996VB21100003},
	author = {McIntosh, L. P. and Hand, G. and Johnson, P. E. and Joshi, M. D. and Korner, M. and Plesniak, L. A. and Ziser, L. and Wakarchuk, W. W. and Withers, S. G.}
}
@article {3838,
	title = {Poly(ethylene glycol) amphiphile adsorption and liposome partition},
	journal = {Journal of Chromatography B-Biomedical Applications},
	volume = {680},
	number = {1-2},
	year = {1996},
	note = {ISI Document Delivery No.: UQ821Times Cited: 4Cited Reference Count: 649th International Conference on Partitioning in Aqueous 2-Phase Systems - Advances in the Use of Polymers in Cell Biology, Biotechnology and Environmental SciencesJUN 04-09, 1995ZARAGOZA, SPAIN},
	month = {May},
	pages = {145-155},
	type = {Proceedings Paper},
	abstract = {Surface localized poly(ethylene glycol) (PEG) amphiphiles of type C-16:0-EO(151) and C-18:2-EO(1.51) were studied via ellipsometry at macroscopic, hat methylated silica (MeSi), phosphatidic acid (PA), and phosphatidylcholine (PC) surfaces. At these surfaces the amphiphiles adsorb similarly, in a non-cooperative manner, achieving a plateau (approximate to 0.1 PEG chains/nm(2)) well below amphiphile critical micelle concentration (CMC). The resultant PEG-enriched layers were 10-15 nm thick, with a polymer concentration (approximate to 0.07 g/cm(3)) greater than the PEG-enriched phase of many dextran, PEG aqueous two-phase systems. PEG-amphiphile adsorption (mg/m(2)) at hydrophobic and phospholipid flat surfaces correlated with changes in the partition (log K) of PC liposomes in such two-phase systems. PEG-amphiphile adsorption at macroscopic surfaces appears to represent a balance between hydrophobic attraction and repulsive intra-chain interactions which promote chain elongation normal to the surface.},
	keywords = {ADSORPTION, AQUEOUS 2-PHASE SYSTEMS, BEHAVIOR, CELL-SEPARATION, critical micelle concentration, ellipsometry, HYDROPHOBIC AFFINITY PARTITION, LIPOSOMES, partitioning, PHASE SYSTEMS, poly(ethylene glycol) (PEG), polymer, PROTEINS, SURFACE-PROPERTIES, WATER-INTERFACE},
	isbn = {0378-4347},
	url = {<Go to ISI>://A1996UQ82100016},
	author = {VanAlstine, J. M. and Malmsten, M. and Brooks, D. E.}
}
@article {3657,
	title = {Solution structure of the ETS domain from murine Ets-1: A winged helix-turn-helix DNA binding motif},
	journal = {Embo Journal},
	volume = {15},
	number = {1},
	year = {1996},
	note = {ISI Document Delivery No.: TQ160Times Cited: 113Cited Reference Count: 68},
	month = {Jan},
	pages = {125-134},
	type = {Article},
	abstract = {Ets-1 is the prototypic member of the ets family of transcription factors, This family is characterized by the conserved ETS domain that mediates specific DNA binding, Using NMR methods, we have determined the structure of a fragment of murine Ets-1 composed of the 85 residue ETS domain and a 25 amino acid extension that ends at its native C-terminus. The ETS domain folds into a helix-turn-helix moth on a four-stranded anti-parallel beta-sheet scaffold. This structure places Ets-1 in the winged helix-turn-helix (wHTH) family of DNA binding proteins and provides a model for interpreting the sequence conservation of the ETS domain and the specific interaction of Ets-1 with DNA. The C-terminal sequence of Ets-1, which is mutated in the v-Ets oncoprotein, forms an alpha-helix that packs anti-parallel to the N-terminal helix of the ETS domain, In this position, the C-terminal helix is poised to interact directly with an N-terminal inhibitory region in Ets-1 as well as the wHTH motif. This explains structurally the concerted role of residues flanking the ETS domain in the intramolecular inhibition of Ets-1 DNA binding.},
	keywords = {AMINO-ACID SUBSTITUTION, C-13, C-ETS-1, COUPLING-CONSTANTS, CRYSTAL-STRUCTURE, DNA binding, ERYTHROBLASTOSIS, FACTORS, GENE FAMILY, intramolecular inhibition, protein NMR structure, PROTEINS, selective labelling, transcription, V-ETS, winged helix-turn-helix},
	isbn = {0261-4189},
	url = {<Go to ISI>://A1996TQ16000013},
	author = {Donaldson, L. W. and Petersen, J. M. and Graves, B. J. and McIntosh, L. P.}
}
@article {3551,
	title = {STRUCTURAL FEATURES OF THE EPSILON-SUBUNIT OF THE ESCHERICHIA-COLI ATP SYNTHASE DETERMINED BY NMR-SPECTROSCOPY},
	journal = {Nature Structural Biology},
	volume = {2},
	number = {11},
	year = {1995},
	note = {ISI Document Delivery No.: TD554Times Cited: 128Cited Reference Count: 43},
	month = {Nov},
	pages = {961-967},
	type = {Article},
	abstract = {The tertiary fold of the epsilon subunit of the Escherichia coli F1F0 ATPsynthase (ECF(1)F(0)) has been determined by two- and three-dimensional heteronuclear (C-13, N-15) NMR spectroscopy. The epsilon subunit exhibits a distinct two domain structure, with the N-terminal 84 residues of the protein forming a 10-stranded beta-structure, and with the C-terminal 48 amino acids arranged as two alpha-helices running antiparallel to one another (two helix hairpin). The beta-domain folds as a beta-sandwich with a hydrophobic interior between the two layers of the sandwich. The C-terminal two-helix hairpin folds back to the N-terminal domain and interacts with one side of the beta-domain. The arrangement of the epsilon subunit in the intact F1F0 ATP synthase involves interaction of the two helix hairpin with the F-1 part, and binding of the open side of the beta-sandwich to the c subunits of the membrane-embedded F-0 part.},
	keywords = {AMINO-ACID-SEQUENCE, CRYOELECTRON MICROSCOPY, EXPRESSION, F1, H+-ATPASE, NUCLEOTIDE, PROTEINS, PROTON, RESOLUTION, TRANSLOCATING ADENOSINE-TRIPHOSPHATASE},
	isbn = {1072-8368},
	url = {<Go to ISI>://A1995TD55400013},
	author = {Wilkens, S. and Dahlquist, F. W. and McIntosh, L. P. and Donaldson, L. W. and Capaldi, R. A.}
}
@article {3106,
	title = {CLONING, SEQUENCING, AND VISCOMETRIC ADHESION ANALYSIS OF HEAT-RESISTANT AGGLUTININ 1, AN INTEGRAL MEMBRANE HEMAGGLUTININ FROM ESCHERICHIA-COLI-O9-H10-K99},
	journal = {Infection and Immunity},
	volume = {62},
	number = {11},
	year = {1994},
	note = {ISI Document Delivery No.: PN304Times Cited: 13Cited Reference Count: 45},
	month = {Nov},
	pages = {5020-5026},
	type = {Article},
	abstract = {The gene encoding a mannose-resistant hemagglutinating protein was cloned from Escherichia coli 09:H10:K99. The hemagglutinin is different from two other mannose-resistant hemagglutinins in this strain, K99 and F41. The agglutinin, named heat-resistant agglutinin 1 (HRA1) since heating to 70 degrees C does not destroy its aggregative properties, strongly agglutinates human, pig, and dog erythrocytes, shows little or no affinity towards cow and chicken erythrocytes, but agglutinates human colon adenocarcinoma 201 (COLO 201) cells. The hra1 gene present on the recombinant plasmid pETE1 was localized by subcloning, and its nucleotide sequence was determined. The gene consists of a 792-bp open reading frame coding for a putative protein of 29 kDa with a predicted N-terminal secretory signal sequence. HRA1 shares no significant identity with data base protein sequences. HRA1 is strongly associated with the bacterial membrane, resisting sonication and isolation attempts based upon standard adhesin purification techniques. N-terminal sequencing of a unique 25-kDa band present in polyacrylamide gels of outer membrane preparations of bacteria harboring pETE1 correlated with the predicted N-terminal amino acid sequence of HRA1 after cleavage of the signal peptide. A viscometric agglutination assay sensitive to the strength of bacterial adhesion shows that the agglutination mediated by bacteria expressing HRA1 is weaker than that of bacteria bearing the F41 adhesin, probably because of the high-molecular-weight, multivalent nature of the latter adhesin. Our observations suggest that HRA1 is a monomeric outer membrane agglutinin.},
	keywords = {ANTIGEN, BACTERIA, DNA, K99, LOCALIZATION, NONFIMBRIAL, OUTER-MEMBRANE, PROTEINS, PURIFICATION, STRAINS},
	isbn = {0019-9567},
	url = {<Go to ISI>://A1994PN30400046},
	author = {Lutwyche, P. and Rupps, R. and Cavanagh, J. and Warren, R. A. J. and Brooks, D. E.}
}
@article {3018,
	title = {SECONDARY STRUCTURE OF THE ETS DOMAIN PLACES MURINE ETS-1 IN THE SUPERFAMILY OF WINGED HELIX-TURN-HELIX DNA-BINDING PROTEINS},
	journal = {Biochemistry},
	volume = {33},
	number = {46},
	year = {1994},
	note = {ISI Document Delivery No.: PT485Times Cited: 59Cited Reference Count: 46},
	month = {Nov},
	pages = {13509-13516},
	type = {Article},
	abstract = {The members of the ets gene family of transcription factors are characterized by a conserved 85-residue DNA-binding region, termed the ETS domain, that lacks sequence homology to structurally characterized DNA-binding motifs. The secondary structure of the ETS domain of murine Ets-1 was determined on the basis of NMR chemical shifts, NOE and J-coupling constraints, amide hydrogen exchange, circular dichroism, and FT-IR spectroscopy. The ETS domain is composed of three a-helices (H) and four beta-strands (S) arranged in the order H1-S1-S2-H2-H3-S3-S4. The four-stranded antiparallel beta-sheet is the scaffold for a putative helix-turn-helix DNA recognition motif formed by helices 2 and 3. The 25 residues extending beyond the ETS domain to the native C-terminus of the truncated Ets-1 also contain a helical segment. On the basis of the similarity of this topology with that of catabolite activator protein (CAP), heat shock factor (HSF), and hepatocyte nuclear factor (HNF-3 gamma), we propose that ets proteins are members of the superfamily of winged helix-turn-helix DNA-binding proteins.},
	keywords = {3-DIMENSIONAL NMR-SPECTROSCOPY, ASSIGNMENT, BACKBONE AMIDE, COUPLING-CONSTANTS, CRYSTAL-STRUCTURE, LARGER, MOTIF, PROTEINS, SIDE-CHAIN RESONANCES, SPECTRA, TRANSCRIPTION FACTORS},
	isbn = {0006-2960},
	url = {<Go to ISI>://A1994PT48500001},
	author = {Donaldson, L. W. and Petersen, J. M. and Graves, B. J. and McIntosh, L. P.}
}
@article {2829,
	title = {COORDINATION CHEMISTRY OF 2-(2{\textquoteright}-HYDROXYPHENYL)-2-BENZOXAZOLE WITH GALLIUM(III) AND ALUMINUM(III) - 2 UNCOMMON GROUP-13 METAL ENVIRONMENTS STABILIZED BY A BIOLOGICALLY RELEVANT BINDING GROUP},
	journal = {Inorganic Chemistry},
	volume = {32},
	number = {22},
	year = {1993},
	note = {ISI Document Delivery No.: ME779Times Cited: 28Cited Reference Count: 36},
	month = {Oct},
	pages = {4909-4913},
	type = {Article},
	abstract = {{The coordination chemistry of Ga(III) and Al(III) with 2-(2{\textquoteright}-hydroxyphenyl)-2-benzoxazole (Hhbo) was investigated both in the solid state (X-ray crystallography) and in solution (H-1, C-13, Al-27 N MR) These two group 13 metal ions exhibit different reactivities toward this bulky bidentate ligand leading with Ga(III) to the formation of Ga(hbo)3 (1) and [Ga(hbo)2(0,0{\textquoteright}-CH3CO2)] (2) complexes depending on the reaction conditions. With AI(III), the only complex formed is[Al(mu-OH)(hbo)2]2(3). The Ga bis(ligand) acetate complex 2 (C28H19GaN2O6) crystallizes in the monoclinic space group C2/c with a = 16.008(3) angstrom},
	keywords = {ACID, AQUEOUS-SOLUTION, COMPLEXES, EQUILIBRIUM, HYDROLYSIS, PERSPECTIVE, PROTEINS, RIBONUCLEOTIDE REDUCTASE, SILICON(IV), SPECIATION},
	isbn = {0020-1669},
	url = {<Go to ISI>://A1993ME77900041},
	author = {Hoveyda, H. R. and Rettig, S. J. and Orvig, Chris}
}
@article {2910,
	title = {FLUORESCENT RESPONSES OF ACRYLODAN-LABELED PLASMA GELSOLIN},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {302},
	number = {1},
	year = {1993},
	note = {ISI Document Delivery No.: KW472Times Cited: 12Cited Reference Count: 24},
	month = {Apr},
	pages = {31-36},
	type = {Article},
	keywords = {ACTIN-BINDING DOMAIN, FILAMENTS, PROTEINS},
	isbn = {0003-9861},
	url = {<Go to ISI>://A1993KW47200005},
	author = {Reid, S. W. and Koepf, E. K. and Burtnick, L. D.}
}
