6 resultados para VELVET ANTLER POLYPEPTIDE

em Archivo Digital para la Docencia y la Investigación - Repositorio Institucional de la Universidad del País Vasco


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Eguíluz, Federico; Merino, Raquel; Olsen, Vickie; Pajares, Eterio; Santamaría, José Miguel (eds.)

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Background: The high demanding computational requirements necessary to carry out protein motion simulations make it difficult to obtain information related to protein motion. On the one hand, molecular dynamics simulation requires huge computational resources to achieve satisfactory motion simulations. On the other hand, less accurate procedures such as interpolation methods, do not generate realistic morphs from the kinematic point of view. Analyzing a protein's movement is very similar to serial robots; thus, it is possible to treat the protein chain as a serial mechanism composed of rotational degrees of freedom. Recently, based on this hypothesis, new methodologies have arisen, based on mechanism and robot kinematics, to simulate protein motion. Probabilistic roadmap method, which discretizes the protein configurational space against a scoring function, or the kinetostatic compliance method that minimizes the torques that appear in bonds, aim to simulate protein motion with a reduced computational cost. Results: In this paper a new viewpoint for protein motion simulation, based on mechanism kinematics is presented. The paper describes a set of methodologies, combining different techniques such as structure normalization normalization processes, simulation algorithms and secondary structure detection procedures. The combination of all these procedures allows to obtain kinematic morphs of proteins achieving a very good computational cost-error rate, while maintaining the biological meaning of the obtained structures and the kinematic viability of the obtained motion. Conclusions: The procedure presented in this paper, implements different modules to perform the simulation of the conformational change suffered by a protein when exerting its function. The combination of a main simulation procedure assisted by a secondary structure process, and a side chain orientation strategy, allows to obtain a fast and reliable simulations of protein motion.

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Lipoproteins are responsible for cholesterol traffic in humans. Low density lipoprotein (LDL) delivers cholesterol from liver to peripheral tissues. A misleading delivery can lead to the formation of atherosclerotic plaques. LDL has a single protein, apoB-100, that binds to a specific receptor. It is known that the failure associated with a deficient protein-receptor binding leads to plaque formation. ApoB-100 is a large single lipid-associated polypeptide difficulting the study of its structure. IR spectroscopy is a technique suitable to follow the different conformational changes produced in apoB-100 because it is not affected by the size of the protein or the turbidity of the sample. We have analyzed LDL spectra of different individuals and shown that, even if there are not big structural changes, a different pattern in the intensity of the band located around 1617 cm 21 related with strands embedded in the lipid monolayer, can be associated with a different conformational rearrangement that could affect to a protein interacting region with the receptor.

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[ES] Durante la excavación de la cueva de Praile Aitz I (Deba, Gipuzkoa) se ha hallado una azagaya de base hendida sobre un suelo de cantos de caliza en el que se definió un contexto de habitación constituido por un hogar, escasos restos de industria y fauna, y varios colgantes. Estos materiales se atribuyen al Magdaleniense Inferior Cantábrico con fechas que se sitúan entre el 15.190 y 15.810 BP. Aprovechando este descubrimiento se realiza una revisión de ejemplares de similares características hallados en otros yacimientos cantábricos (Balmori, El Castillo) y se plantea la posible cronología magdaleniense del ejemplar de Santimamiñe.

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Este trabajo ha sido realizado en el marco del Grupo de Investigación Consolidado GIC 07/21-IT.288.07.

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[ES] La cueva de Gatzarria ofrece un rico e interesante relleno del Paleolítico medio y superior. La industria ósea «elaborada» (puntas,puntas en extremo, alisadores y varillas) se halla documentada en los niveles Protoauriñacienses (cjn2 y cjnl), en el Auriñaciense antiguo de cbci-cbf y en el Autiñaciense evolucionado de cb. De todas las categorías atestiguadas que aquí tratamos, el grupo más numeroso e interesante es el de las puntas: junto a una serie de ejemplares sin denominación específica que se repiten en los mencionados niveles, existen algunos tipos ligados específicamente a algunos de ellos; es el caso de las puntas fusiformes en cjn2, de las puntas sublosángicas en cjnl y de las puntas de base hendida en cbci-cbf.