11,475 research outputs found
Bernard Williams
No full textAn edited multi-author volume assessing the moral philosophy of the late British philosopher Bernard Williams. Contributors: Adrian Moore, John Skorupski, Alan Thomas, Robert B Louden, Michael Stocker, A. A. Long, Edward Crai
An open reply to "What is going on at the Library of Congress?" by Thomas Mann
No full textThis is an open response to a report by Thomas Mann at the Library of Congress concerning changes in cataloging. The author contends that, although the current changes at the Library of Congress are suspect, changes are imminent and experienced catalogers must offer positive suggestions for change, otherwise they will be ignored by management
Measurement of the Xi(-)(b) and Omega(-)(b) baryon lifetimes
No full textUsing a data sample of pp collisions corresponding to an integrated luminosity of 3 fb−1, the Ξ−b and Ω−b baryons are reconstructed in the Ξ−b → J/ψΞ− and Ω−b → J/ψΩ− decay modes and their lifetimes measured to be
τ(Ξ−b) = 1.55+0.10−0.09 (stat) ± 0.03 (syst) ps,
τ(Ω−b) = 1.54+0.26−0.21 (stat) ± 0.05 (syst) ps.
These are the most precise determinations to date. Both measurements are in good agreement with previous experimental results and with theoretical predictions
Measurement of the ratio of branching fractions B(B0→K∗0γ )/B(B0s→φγ ) and the directCP asymmetry inB 0→K∗0γ
No full textThe ratio of branching fractions of the radiative B decays B0→K⁎0γ and B0s→ϕγ has been measured using an integrated luminosity of 1.0 fb−1 of pp collision data collected by the LHCb experiment at a centre-of-mass energy of s√=7TeV. The value obtained is
B(B0→K⁎0γ)B(B0s→ϕγ)=1.23±0.06(stat.)±0.04(syst.)±0.10(fs/fd),
where the first uncertainty is statistical, the second is the experimental systematic uncertainty and the third is associated with the ratio of fragmentation fractions fs/fd. Using the world average value for B(B0→K⁎0γ), the branching fraction B(B0s→ϕγ) is measured to be (3.5±0.4)×10−5.
The direct CP asymmetry in B0→K⁎0γ decays has also been measured with the same data and found to be
ACP(B0→K⁎0γ)=(0.8±1.7(stat.)±0.9(syst.))%.
Both measurements are the most precise to date and are in agreement with the previous experimental results and theoretical expectations
Structure of a bacterial pyridoxal 5'-phosphate synthase complex
No full textVitamin B6 is an essential metabolic cofactor that has more functions in humans than any other single nutrient. Its de novo biosynthesis occurs through two mutually exclusive pathways that are absent in animals. The predominant pathway found in most prokaryotes, fungi, and plants has only recently been discovered. It is distinguished by a glutamine amidotransferase, which is remarkable in that it alone can synthesize the cofactor form, pyridoxal 5'-phosphate (PLP), directly from a triose and a pentose saccharide and glutamine. Here we report the 3D structure of the PLP synthase complex with substrate glutamine bound as well as those of the individual synthase and glutaminase subunits Pdx1 and Pdx2, respectively. The complex is made up of 24 protein units assembled like a cogwheel, a dodecameric Pdx1 to which 12 Pdx2 subunits attach. In contrast to the architecture of previously determined glutamine amidotransferases, macromolecular assembly is directed by an N-terminal alpha-helix on the synthase. Interaction with the synthase subunit leads to glutaminase activation, resulting in formation of an oxyanion hole, a prerequisite for catalysis. Mutagenesis permitted identification of the remote glutaminase and synthase catalytic centers and led us to propose a mechanism whereby ammonia shuttles between these active sites through a methionine-rich hydrophobic tunnel
Pedo-geophysics teaching and research in the Adelaide hills
No full textPlease see page 6 of PDF for this item.Graham Heinson, Nick Direen, Mark Thomas, Andrew Baker, Rob Fitzpatrick, Patrick James, Brendan Coleman, Matthew Hutchens, Hashim Carey and the 3rd year Mineral and Environmental Geophysics Clas
Two independent routes of de novo vitamin B6 biosynthesis: not that different after all
No full textVitamin B6 is well known in its biochemically active form as pyridoxal 5'-phosphate, an essential cofactor of numerous metabolic enzymes. The vitamin is also implicated in numerous human body functions ranging from modulation of hormone function to its recent discovery as a potent antioxidant. Its de novo biosynthesis occurs only in bacteria, fungi and plants, making it an essential nutrient in the human diet. Despite its paramount importance, its biosynthesis was predominantly investigated in Escherichia coli, where it is synthesized from the condensation of deoxyxylulose 5-phosphate and 4-phosphohydroxy-L-threonine catalysed by the concerted action of PdxA and PdxJ. However, it has now become clear that the majority of organisms capable of producing this vitamin do so via a different route, involving precursors from glycolysis and the pentose phosphate pathway. This alternative pathway is characterized by the presence of two genes, Pdx1 and Pdx2. Their discovery has sparked renewed interest in vitamin B6, and numerous studies have been conducted over the last few years to characterize the new biosynthesis pathway. Indeed, enormous progress has been made in defining the nature of the enzymes involved in both pathways, and important insights have been provided into their mechanisms of action. In the present review, we summarize the recent advances in our knowledge of the biosynthesis of this versatile molecule and compare the two independent routes to the biosynthesis of vitamin B6. Surprisingly, this comparison reveals that the key biosynthetic enzymes of both pathways are, in fact, very similar both structurally and mechanistically
Thomas Roy McLean
No full textNotes - This is the story of Mr. Thomas Roy McLean - his marriage to Helen, his life in Hay River and Athabasca, and his careers in radio and at the creamery. Mr. McLean ran an appliance store in Athabasca and was part of bringing electricity to the area. His store and neighbouring businesses are described in great detail in this document (3 pages
A compleat collection of devotions : both publick and private : taken from the apostolical constitutions, the ancient liturgies, and the Common prayer book of the Church of England ... [etc.].
No full textSignatures: [pi]¹, A?, A-Y?, Z?, a-h?, i? (final verso blank).; Attributed to Thomas Deacon.; Label: Library of the Congregation of U.B. of the Borough of Bethlehem and its vicinity, no. 877.; Signature; B. Ingham.; An appendix in justification of the foregoing undertaking ... has separate title and pagings.; BM,; ESTC
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