1000 resultados para 175-1084C
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The role of invariant water molecules in the activity of plant cysteine protease is ubiquitous in nature. On analysing the 11 different Protein DataBank (PDB) structures of plant thiol proteases, the two invariant water molecules W I and W2 (W220 and W222 in the template 1PPN structure) were observed to form H-bonds with the Ob atom of Asn 175. Extensive energy minimization and molecular dynamics simulation studies up to 2 ns on all the PDB and solvated structures clearly revealed the involvement of the H-bonding association of the two water molecules in fixing the orientation of the asparagine residue of the catalytic triad. From this study, it is suggested that H-bonding of the water molecule at the W1 invariant site better stabilizes the Asn residue at the active site of the catalytic triad.
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Contenido: La prudencia (I) / Octavio Nicolás Derisi – Sujeto, acto y operación / Daniel Gamarra – Sobre la naturaleza de los “derechos” / Héctor H. Hernández – Decir lo mismo (Frege y Santo Tomás) / Juan J. Sanguineti – La teoría del tiempo en Ockham y la autenticidad de la Summulae in Libros Physicorum / Olga L. Larre ; J. E. Bolzán – Filosofía cristiana y apologética en Mons. Audino Rodríguez y Olmos / Alberto Caturelli – Notas y comentarios -- Bibliografía
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Consultoria Legislativa - Área IV - Matéria Orçamentária Pública.
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The neutron deficient nuclide Ir-175 was produced by irradiation of Nd-146 with 210 MeV Cl-35 via a fusion-evaporation reaction channel. The reaction products were transported to a low-background location using a helium-jet recoil fast-moving tape-transport system for measurement. The experimental devices and data analysis method are introduced. Based on the decay-curve fitting of the beta-delayed gamma ray from Ir-175, realized by the least-square method, a new long-lived isomeric state of Ir-175 is proposed and briefly discussed.
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57 fotografías, cicuenta y cuatro a color.