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Article Dans Une Revue Journal de Physique Année : 1989

Statistical mechanics model of protein folding : short and long chains have different folding transitions

Résumé

A statistical mechanics model of a polypeptide chain is used to simulate the folding process. Each residue is defined by a set of independent characters within a given sequence. Simulations of this model in a mean-field (infinite-dimensional) geometry show that (i) short chains do not fold, (ii) medium chains fold according to a spin-glass-like « transition » (where most characters must be partially satisfied) and (iii) long chains fold according to a Mattis-like « transition » (where only one dominant character is almost completely satisfied). This change in folding mechanism associated to chain length may be relevant to the existence of multidomain proteins.

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jpa-00211125 , version 1 (04-02-2008)

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J.-R. Garel, T. Garel, Henri Orland. Statistical mechanics model of protein folding : short and long chains have different folding transitions. Journal de Physique, 1989, 50, pp.3067-3074. ⟨10.1051/jphys:0198900500200306700⟩. ⟨jpa-00211125⟩
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