984 resultados para 1995_12051933 CTD-36 5400712
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An efficient strategy for the contruction of spiro[4.5] decanes is described and involves a bridgehead substitution of a methoxyl group by a methyl group followed by an oxidative cleavage of the tricyclo[5.2.2.0(1,5)] undecane 25 to produce the spiro[4.5] decanes 31 & 32 which are intermediates in the synthesis of acorone. A novel one-pot conversion of alpha-methoxy carboxylic acid to alpha-methyl carboxylic acid is described.
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Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase. GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST). GC-C is also expressed in neurons, where it plays a role in satiation and attention deficiency/hyperactive behavior. GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity. When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished. Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation. We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36. Interaction with VIP36 is dependent on glycosylation at the same sites that allow GC-C to fold and bind ligand. Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
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The protein folding funnel paradigm suggests that folding and unfolding proceed as directed diffusion in a multidimensional free energy surface where a multitude of pathways can be traversed during the protein's sojourn from initial to final state. However, finding even a single pathway, with the detail chronicling of intermediates, is an arduous task. In this work we explore the free energy surface of unfolding pathway through umbrella sampling, for a small globular a-helical protein chicken-villin headpiece (HP-36) when the melting of secondary structures is induced by adding DMSO in aqueous solution. We find that the unfolding proceeds through the initial separation or melting of aggregated hydrophobic core that comprises of three phenylalanine residues (Phe7, Phe11, and Phe18). This separation is accompanied by simultaneous melting of the second helix. Unfolding is found to be a multistage process involving crossing of three consecutive minima and two barriers at the initial stage. At a molecular level, Phe18 is observed to reorient itself towards other hydrophobic grooves to stabilize the intermediate states. We identify the configuration of the intermediates and correlate the intermediates with those obtained in our previous works. We also give an estimate of the barriers for different transition states and observe the softening of the barriers with increasing DMSO concentration. We show that higher concentration of DMSO tunes the unfolding pathway by destabilizing the third minimum and stabilizing the second one, indicating the development of a solvent modified, less rugged pathway. The prime outcome of this work is the demonstration that mixed solvents can profoundly transform the nature of the energy landscape and induce unfolding via a modified route. A successful application of Kramer's rate equation correlating the free energy simulation results shows faster rate of unfolding with increasing DMSO concentration. This work perhaps presents the first systematic theoretical study of the effect of a chemical denaturant on the microscopic free energy surface and rates of unfolding of HP-36. (C) 2014 AIP Publishing LLC.
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Contenido: La inserción de la universidad en el medio : país e Iglesia / Domingo Basso – Reflexiones en torno al ser y al hacer de las universidades católicas / Jorge Humberto Peláez – La Constitución y los tratados internacionales a partir de la reforma de 1994 / Eugenio Luis Palazzo – Los Iudicia Bonae Fidei y su importancia en materia contractual / Alberto Gustavo Di Pietro – En torno a Pro Caccina / Edmundo J. Carbone – Los iuris praecepta o la norma ética como imperativo jurídico / Ángel Hugo Guerriero – La objetividad en el saber político / Héctor Julio Martinotti – Presencia de la Iglesia en la universidad y en la cultura universitaria / Pío Laghi ; Eduardo Pironio ; Paul Poupard – III Encuentro Internacional de Derecho de América del Sur. “El derecho y la integración hacia el siglo XXI”. “Pasos previos para la integración política de América Latina” / Flavio Fernando Agatiello Piñero
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Fecha: >1970 / Unidad de instalación: Carpeta 48 - Expediente 7-14 / Nº de pág.: 3 (mecanografiadas)
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*Table of Contents* Research & farming techniques Nursery rearing of Puntius goniotus: A preliminary trial K.N. Mohnta, J.K. Jena & S.N. Mohanty Artemia enrichment and biomass production for larval finfish and shellfish culture A.S. Ninawe Vembanad Lake: A potential spawner bank of the giant freshwater prawn Macrobrachium rosenbergii on the southwest coast of India Paramaraj Balamurugan, Pitchaimuthu Mariappan & Chellam Balasundaram Seed production of mud crab Scylla serrata at the Rajiv Gandhi Center for Aquaculture, Tamil Nadu, India Mohamed Shaji, Emilia T. Quinitio, Thampi Samraj, S. Kandan, K. Ganesh, Dinesh Kumar, S. Arulraj, S. Pandiarajan, Shajina Ismail and K. Dhandapan. Sustainable aquaculture Fish wastes in urban and suburban markets of Kolkata: Problems and potentials Kausik Mondal, Anilava Kaviraj & P.K. Mukhopadhyay People in aquaculture Peter Edwards writes on rural aquaculture: Farming carps in leased ponds by groups of poor women in Chandpur, Bangladesh Aquatic animal health Lymphocystis disease and diagnostic methods in China Jing Xing, Xiuzhen Sheng & Wenbin Zhan Asia-Pacific Marine Finfish Aquaculture Network Mesocosm technology advances grouper culture in northern Australia Elizabeth Cox, Peter Fry & Anjanette Johnston
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Linker histone H1 plays an important role in chromatin folding. Phosphorylation by cyclin-dependent kinases is the main post-translational modification of histone H1. We studied the effects of phosphorylation on the secondary structure of the DNA-bound H1 carboxy-terminal domain (CTD), which contains most of the phosphorylation sites of the molecule. The effects of phosphorylation on the secondary structure of the DNA-bound CTD were site-specific and depended on the number of phosphate groups. Full phosphorylation significantly increased the proportion of -structure and decreased that of -helix. Partial phosphorylation increased the amount of undefined structure and decreased that of -helix without a significant increase in -structure. Phosphorylation had a moderate effect on the affinity of the CTD for the DNA, which was proportional to the number of phosphate groups. Partial phosphorylation drastically reduced the aggregation of DNA fragments by the CTD, but full phosphorylation restored to a large extent the aggregation capacity of the unphosphorylated domain. These results support the involvement of H1 hyperphosphorylation in metaphase chromatin condensation and of H1 partial phosphorylation in interphase chromatin relaxation. More generally, our results suggest that the effects of phosphorylation are mediated by specific structural changes and are not simply a consequence of the net charge.
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Sediment samples were taken from Lake Langans in Sweden and fossilised diatoms analysed. Sample methods and environmental factors are discussed. Species with a characteristic occurrence are described. The article discusses diatom-thanatocoenoses as indicators of environment.