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À propos de : Energy landscape and dynamics of an HP lattice model of proteins —The role of anisotropy        

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  • Energy landscape and dynamics of an HP lattice model of proteins —The role of anisotropy
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  • We present the results of exact numerical studies of the energy landscape and the dynamics of a 12-monomer chain comprised of two types of amino acids called the HP model. We benchmark our findings against the corresponding results of previous studies of a Go model, which encodes the native state conformation. We also show how the energy landscape gets modified dramatically and improves the folding properties on incorporating the inherent anisotropy of a chain, albeit in a simplified manner.
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  • epl15929
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  • © EPLA, 2013
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