Titlebook: Aspects of Physical Biology; Biological Water, Pr G. Franzese,M. Rubi Book 2008 Springer-Verlag Berlin Heidelberg 2008 ATPase.active transp

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BILK

Joe David,Eric Coatanéa,Andrei Lobovlifetimes. These clusters have a higher free energy than the protein solution, and their lifetime is determined by a barrier for their decay. The clusters affect the viscous and visco-elastic behavior of the solution and are an essential part of potential condensation and aggregation pathways. Since

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Rizwan Ullah,Eric Fangnon,Juha Huukient by varying the strength of inter-bead interactions can speed up simulations sufficiently to generate many folding–unfolding events and to track the aggregation of many peptides. This increase in speed is gained mainly due to the ballistic motion of either secondary structures of the protein or i

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J. Hollingum,K. Kobayashi,H. Inabaesis coefficients. They are all probably significant. We discuss that the complete set of coefficients can explain slippage in molecular pumps as well as thermogenesis that is triggered by a temperature jump.

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,Ma?nahmen zur Erh?hung der Mengenleistung,nformation propagates in a cortex slice via an avalanche mode. Both features have been found in other problems in the context of the physics of complex systems and successful models have been developed to describe their behavior. In this contribution, we apply a statistical mechanical model to descr

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Anomalous Behaviour of Supercooled Water and Its Implication for Protein Dynamicsrol mixtures that support this slaving idea. Moreover, we show how confined supercooled water changes its dynamical behaviour from a low temperature Arrhenius behaviour to a high temperature non-Arrhenius behaviour at a certain temperature (around 200 K), and then we discuss likely explanations for

PHAG

Interactions of Polarizable Media inWater and the Hydrophobic Interactione biomolecules regarding polarizability, an effect that may be relevant for understanding the conformational changes of proteins and other biomolecules in solution. In this chapter, we provide a critical discussion of the current state of hydrophobic interactions, with particular emphasis on biomole

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Metastable Mesoscopic Phases in Concentrated Protein Solutionslifetimes. These clusters have a higher free energy than the protein solution, and their lifetime is determined by a barrier for their decay. The clusters affect the viscous and visco-elastic behavior of the solution and are an essential part of potential condensation and aggregation pathways. Since