Geometry of the energy landscape and folding transition in a simple model of a protein

Details Geometry of the energy landscape and folding transition in a simple model of a protein Geometry of the energy landscape and folding transition in a simple model of a protein

2008-04-22

arxiv.org/abs/0804.3576v1

Physics

Condensed Matter

Statistical Mechanics

to appear in Physical Review E

Scientific paper

10.1103/PhysRevE.77.051917

A geometric analysis of the global properties of the energy landscape of a minimalistic model of a polypeptide is presented, which is based on the relation between dynamical trajectories and geodesics of a suitable manifold, whose metric is completely determined by the potential energy. We consider different sequences, some with a definite protein-like behavior, a unique native state and a folding transition, and the others undergoing a hydrophobic collapse with no tendency to a unique native state. The global geometry of the energy landscape appears to contain relevant information on the behavior of the various sequences: in particular, the fluctuations of the curvature of the energy landscape, measured by means of numerical simulations, clearly mark the folding transition and allow to distinguish the protein-like sequences from the others.

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