997 resultados para Sligh, Charles Robert, 1906-
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A by-law begins: "It was then moved by R.S. Kinner and Seconded by George Barnes that by Law No. 12 be read. Whereas by Identure bearing date thirteenth day of August A.D. 1873 made between one George Barnes of the first part thereof and Andrew S. Kinner and Charles Robert Murray of the second part thereof which said Identure was duly registered in the Registry Office for Lands for the said County of Lincoln on the 14th day of August A.D. 1880 in Book 4 for the Township of Louth as No. 1534 the said George Barnes granted and conveyed the Lands and premises therein described to the said Andrew S. Kinner and Charles Robert Murray and their heirs and assigns as joint tenants and not as tenants as common upon the trusts and for the purposes therein expressed. And Whereas the said Andrew S. Kinner died on about the 13th day of June 1877 A.D. without having made any appointment under the provisions of the said in part recited Identure.."
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Toutes les illustrations qui ponctuent cette thèse ont été réalisées par Chantal Poirier. Elles ont été insérées dans le texte selon un ordre méticuleusement aléatoire.
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Mémoire numérisé par la Division de la gestion de documents et des archives de l'Université de Montréal
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The structure of tick anticoagulant peptide (TAP) has been determined by X-ray crystallography at t.6 Å resolution complexed with bovine pancreatic trypsin inhibitor (BPTI). The TAP-BPTI crystals are tetragonal, a = b = 46.87, c = 50.35 Å, space group P41, four complexes per unit cell. The TAP molecules are highly dipolar and form an intermolecular helical array along the c-axis with a diameter of about 45 Å. Individual TAP units interact in a head-to-tail fashion, the positive end of one molecule associating with the distal negative end of another, and vice versa. The BPTI molecules have a uniformly distributed positively charged surface that interacts extensively through 14 hydrogen bonds and two hydrogen bonded salt bridges with the helical groove around the helical TAP chains. Comparing the structure of TAP in TAP-BPTI with TAP bound to factor Xa(Xa) suggests a massive reorganization in the N-terminal tetrapeptide and the first disulfide loop of TAP (CyS5(T)- Cys 15(T)) upon binding to Xa. The Tyr1(T)OH atom of TAP moves 14.2 Å to interact with Asp189 of the S1 specificity site, Arg3(T)CZ moves 5.0 Å with the guanidinium group forming a cation-π-electron complex in the S4 subsite of Xa, while Lys7(T)NZ differs in position by 10.6 Å in TAP-BPTI and TAP-Xa, all of which indicates a different pre-Xa-bound conformation for the N- terminal of TAP in its native state. In contrast to TAP, the BPTI structure of TAP-BPTI is practically the same as all those of previously determined structures of BPTI, only arginine and lysine side-chain conformations showing significant differences.
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Pós-graduação em Educação - IBRC
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R. H. Charles
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Charles L. Hallgarten
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R. Türke
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Von R. Pilger
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Fil: Prati, Marcelo. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.
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Fil: Prati, Marcelo. Universidad Nacional de La Plata. Facultad de Humanidades y Ciencias de la Educación; Argentina.
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Shipping list no.: 95-0278-P.
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Mode of access: Internet.