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

• Main Authors: Mazzoni, Lorenzo N, Casetti, Lapo
• Format: Journal Article
• Language: English
• Published: 22-04-2008
• Subjects: Physics - Soft Condensed Matter; Physics - Statistical Mechanics; Quantitative Biology - Biomolecules
• DOI: 10.48550/arxiv.0804.3576

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.