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14,306 items found (0 items not approved), displaying 61 to 70.[First/Prev] 3, 4, 5, 6, 7, 8, 9, 10 [Next/Last]

Instruments / Technical Area	Publication Details	Published	Actions
	Effect of 4-fluoro-L-proline on the SH3 binding affinity Paolo Ruzza , Chiara Rubini , Andrea Calderan , Andrea Guiotto , Luca Cesaro , Anna M. Brunati , Arianna Donella-Deana , Rohanah Hussain , Giuliano Siligardi Peptides For Youth: The Proceedings Of The 20th American Peptide Symposium 611, 499-500 20th American Peptide Symposium DOI: 10.1007/978-0-387-73657-0_216 PMID: 19400283	Mar 2009
	The crystal structures of the low-temperature and high-pressure polymorphs of nitric acid D. R. Allan , W. G. Marshall , D. J. Francis , I. D. H. Oswald , C. Spanswick , C. R. Pulham Dalton Transactions 39 (15), 3736-3743 DOI: 10.1039/b923975h PMID: 20354626 Show Abstract ▼ Abstract: A new high-pressure phase of pure nitric acid (HNO(3)) has been characterised at 1.6 GPa at room temperature by high-pressure neutron powder and X-ray single-crystal diffraction techniques. This is the first crystalline phase obtained upon compression of liquid nitric acid at room temperature and appears to be the stable phase up to pressures of at least 4 GPa. The crystal structure of this new phase shows some similarities to that of the low-temperature phase of nitric acid at ambient pressure, which has been redetermined as part of this study. Both structures share a herringbone packing of hydrogen-bonded molecular catemers, although the presence of disorder within the hydrogen bonds within one of the catemers of the low-temperature phase makes its structure comparatively more complex.	Mar 2010
	First Year's Experience of Diamond's Insertion Devices Emily Longhi , Riccardo Bartolini , Richard Fielder 11th European Parcticle Accelerator Conference	Jun 2008
	Crystal Structure of the Acid Induced Arginine Decarboxylase from Escherichia coli: Reversible Decamer Assembly Controls Enzyme Activity Juni Andrell , Matthew Hicks , Tracy Palmer , Liz Carpenter , So Iwata , Megan Maher Biochemistry DOI: 10.1139/O09-182 PMID: 20453931 Diamond Proposal Number(s): [316] Show Abstract ▼ Abstract: Enteric bacteria such as Escherichia coli have acquired a wide array of acid stress response systems to counteract the extreme acidity encountered when invading the host's digestive or urinary tracts. These acid stress response systems are both enzyme and chaperone based. The 3 main enzyme-based acid resistance pathways are glutamate-, arginine-, and lysine-decarboxylase pathways. They are under a complex regulatory network allowing the bacteria to fine tune its response to the external environment. HdeA and HdeB are the main chaperones involved in acid stress response. The decarboxylase systems are also found in Vibrio cholera, Vibrio vulnifus, Shigella flexneri. and Salmonella typhimurium, although some differences exist in their functional mechanism and regulation.	Mar 2009
	Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site. Jonathan Ruprecht , Victoria Yankovskaya , Elena Maklashina , So Iwata , Gary Cecchini Journal Of Biological Chemistry DOI: 10.1074/jbc.M109.010058 Diamond Proposal Number(s): [316] Show Abstract ▼ Abstract: Three new structures of Escherichia coli succinate-quinone oxidoreductase (SQR) have been solved. One with the specific quinone-binding site (Q-site) inhibitor carboxin present has been solved at 2.4 Å resolution and reveals how carboxin inhibits the Q-site. The other new structures are with the Q-site inhibitor pentachlorophenol and with an empty Q-site. These structures reveal important details unresolved in earlier structures. Comparison of the new SQR structures shows how subtle rearrangements of the quinone-binding site accommodate the different inhibitors. The position of conserved water molecules near the quinone binding pocket leads to a reassessment of possible water-mediated proton uptake networks that complete reduction of ubiquinone. The dicarboxylate-binding site in the soluble domain of SQR is highly similar to that seen in high resolution structures of avian SQR (PDB 2H88) and soluble flavocytochrome c (PDB 1QJD) showing mechanistically significant structural features conserved across prokaryotic and eukaryotic SQRs.	Aug 2009
	Analysis of time-resolved energy-dispersive X-ray absorption spectroscopy data for the study of chemical reaction intermediate states D. T. Bowron , S. Diaz-Moreno Analytical Chemistry 77 (19), 6445 DOI: 10.1021/ac050954d Show Abstract ▼ Abstract: Energy-dispersive X-ray absorption spectroscopy is an increasingly powerful tool for the investigation of kinetic processes in chemical systems as an element-specific local structure and electronic-state probe. Advances in synchrotron radiation sources and detector technology are pushing the time resolution of the method to ever shorter periods, currently milliseconds to microseconds, while also providing a concomitant improvement in data quality that now makes feasible the identification of structural and electronic motifs characteristic of intermediate states in chemical processes. To maximize the value of the newly available high-quality time-resolved data, techniques for consistent data normalization and structural component analysis have been developed and here are illustrated in a model study of the electron-transfer reaction between [IrCl6]2- with [Co(CN)5]3-.	Aug 2005
	Today's wastes, tomorrow's materials for environmental protection L. E. Macaskie , I. P. Mikheenko , P. Yong , K. Deplanche , M. Paterson-Beedle , V. S. Coker , C. I. Pearce , R. A. D. Pattrick , D. Vaughan , G. Van Der Laan , J. R. Lloyd Advanced Materials Research 71-73, 541-548 DOI: 10.4028/www.scientific.net/AMR.71-73.541 Show Abstract ▼ Abstract: Over the past 30 years the literature has burgeoned with bioremediation approaches to heavy metal removal from wastes. The price of base and precious metals has dramatically increased. With the resurgence of nuclear energy uranium has become a strategic resource. Other ‘non-carbon energy’ technologies are driven by the need to reduce CO2 emissions. The ‘New Biohydrometallurgy’ we describe unites these drivers by the concept of conversion of wastes into new materials for environmental applications. The new materials, fashioned, bottom-up, into nanomaterials under biocontrol, can be termed ‘Functional Bionanomaterials’. This new discipline, encompassing waste treatment along with nanocatalysis or other applications, can be summarized as ‘Environmental Bionanotechnology’. Several case histories illustrate the scope and potential of this concept.	May 2009
	Insights into how nucleotide-binding domains power ABC transport Philip W. Fowler , Paul Bilton , Elizabeth P. Carpenter , Peter J. Sadler , Dominic J. Campopiano , Mark S. P. Sansom , So Iwata , Simon Newstead Structure 17 (9), 1213-22. DOI: 10.1016/j.str.2009.07.009 PMID: 19748342 Diamond Proposal Number(s): [316] Open Access Show Abstract ▼ Abstract: The mechanism by which nucleotide-binding domains (NBDs) of ABC transporters power the transport of substrates across cell membranes is currently unclear. Here we report the crystal structure of an NBD, FbpC, from the Neisseria gonorrhoeae ferric iron uptake transporter with an unusual and substantial domain swap in the C-terminal regulatory domain. This entanglement suggests that FbpC is unable to open to the same extent as the homologous protein MalK. Using molecular dynamics we demonstrate that this is not the case: both NBDs open rapidly once ATP is removed. We conclude from this result that the closed structures of FbpC and MalK have higher free energies than their respective open states. This result has important implications for our understanding of the mechanism of power generation in ABC transporters, because the unwinding of this free energy ensures that the opening of these two NBDs is also powered.	Sep 2009
	Structural investigation of the bridged activated complex in the reaction between hexachloroiridate(IV) and pentacyanocobaltate(II) Sofia Diaz-Moreno , Daniel T. Bowron , John Evans Dalton Transactions 3814 DOI: 10.1039/b507738a PMID: 16471065 Show Abstract ▼ Abstract: Time resolved energy dispersive X-ray absorption spectroscopy has been used to follow the structural evolution of the inner-sphere electron transfer reaction between [IrCl6]2− and [Co(CN)5]3−, and to characterise the local structure of the iridium metal centre in the bridged activated complex formed during the reaction.	Sep 2005
	Reconstitution in vitro of the catalytic portion (NtpA3-B3-D-G complex) of Enterococcus hirae V-type Na+-ATPase S. Arai , I. Yamato , A. Saijo , Y. Kakinuma , Y. Ishizuka-Katsura , M. Toyama , T. Terada , M. Shirouzu , S. Yokoyama , S. Iwata , T. Murata Biochemical And Biophysical Research Communications DOI: 10.1016/j.bbrc.2009.10.032 Diamond Proposal Number(s): [316] Show Abstract ▼ Abstract: Enterococcus hirae vacuolar ATPase (V-ATPase) is composed of a soluble catalytic domain (V1; NtpA3-B3-D-G) and an integral membrane domain (V0; NtpI-K10) connected by a central and peripheral stalk(s) (NtpC and NtpE-F). Here we examined the nucleotide binding of NtpA monomer, NtpB monomer or NtpD-G heterodimer purified by using Escherichia coli expression system in vivo or in vitro, and the reconstitution of the V1 portion with these polypeptides. The affinity of nucleotide binding to NtpA was 6.6 ?M for ADP or 3.1 ?M for ATP, while NtpB or NtpD-G did not show any binding. The NtpA and NtpB monomers assembled into NtpA3-B3 heterohexamer in nucleotide binding-dependent manner. NtpD-G bound NtpA3-B3 forming V1 (NtpA3-B3-D-G) complex independent of nucleotides. The V1 formation from individual NtpA and NtpB monomers with NtpD-G heterodimer was absolutely dependent on nucleotides. The ATPase activity of reconstituted V1 complex was as high as that of native V1-ATPase purified from the V0V1 complex by EDTA treatment of cell membrane. This in vitro reconstitution system of E. hirae V1 complex will be valuable for characterizing the subunit-subunit interactions and assembly mechanism of the V1-ATPase complex.	Dec 2009

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