Isbn: 9783838107714 - explicit solvent effects on protein physics: modeling lattice proteins in aqueous environments (4 resultados)

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  • Idioma: Inglés

    Editorial: Südwestdeutscher Verlag Für Hochschulschriften AG Co. KG Sep 2015, 2015

    3838107713 / 9783838107714

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    Librería: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, AlemaniaBuchWeltWeit Ludwig Meier e.K.

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    Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Protein folding stands as one of the major interdisciplinary challenges of the last fifteen years, involving biology, chemistry, medicine and physics. In this book solvent effects, and the related hydrophobic effect, on proteins are investigated. Using a simple lattice model of proteins, in which the solvent is semi-explicitly taken into account, thermodynamical quantities can be investigated and the crucial role the solvent plays in protein folding can be demonstrated. Of particular relevance is our observation that a simple model, in which the potential energy is described in terms of the interactions between amino-acids only, does not correctly reproduce solvent effects. Approaches like this, in which solvent effects are treated implicitly, are commonly employed in many of more sophisticated models for protein folding dynamics. Our results are then of great importance as they suggest the treatment of the solvent in these models may need to be re-examined. 108 pp. Deutsch.…

  • Idioma: Inglés

    Editorial: Südwestdeutscher Verlag für Hochschulschriften, 2015

    3838107713 / 9783838107714

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    Librería: moluna, Greven, Alemaniamoluna

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    Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Protein folding stands as one of the major interdisciplinary challenges of the last fifteen years, involving biology, chemistry, medicine and physics. In this book solvent effects, and the related hydrophobic effect, on proteins are investigated. Using a si.…

  • Idioma: Inglés

    Editorial: Südwestdeutscher Verlag Für Hochschulschriften Jul 2009, 2009

    3838107713 / 9783838107714

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    Librería: buchversandmimpf2000, Emtmannsberg, BAYE, Alemaniabuchversandmimpf2000

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    Taschenbuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Protein folding stands as one of the major interdisciplinary challenges of the last fifteen years, involving biology, chemistry, medicine and physics. In this book solvent effects, and the related hydrophobic effect, on proteins are investigated. Using a simple lattice model of proteins, in which the solvent is semi-explicitly taken into account, thermodynamical quantities can be investigated and the crucial role the solvent plays in protein folding can be demonstrated. Of particular relevance is our observation that a simple model, in which the potential energy is described in terms of the interactions between amino-acids only, does not correctly reproduce solvent effects. Approaches like this, in which solvent effects are treated implicitly, are commonly employed in many of more sophisticated models for protein folding dynamics. Our results are then of great importance as they suggest the treatment of the solvent in these models may need to be re-examined.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 108 pp. Deutsch.…

  • Idioma: Inglés

    Editorial: Südwestdeutscher Verlag Für Hochschulschriften, 2009

    3838107713 / 9783838107714

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    Librería: AHA-BUCH GmbH, Einbeck, AlemaniaAHA-BUCH GmbH

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    Condición: Nuevo

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    Cantidad disponible: 1 disponible

    Taschenbuch. Condición: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Protein folding stands as one of the major interdisciplinary challenges of the last fifteen years, involving biology, chemistry, medicine and physics. In this book solvent effects, and the related hydrophobic effect, on proteins are investigated. Using a simple lattice model of proteins, in which the solvent is semi-explicitly taken into account, thermodynamical quantities can be investigated and the crucial role the solvent plays in protein folding can be demonstrated. Of particular relevance is our observation that a simple model, in which the potential energy is described in terms of the interactions between amino-acids only, does not correctly reproduce solvent effects. Approaches like this, in which solvent effects are treated implicitly, are commonly employed in many of more sophisticated models for protein folding dynamics. Our results are then of great importance as they suggest the treatment of the solvent in these models may need to be re-examined.…