Local entropy in proteins.

ABSTRACT: Proteins populate dynamic ensembles, yet how temperature and mutations reshape these ensembles remains poorly understood. We introduce a local entropy metric that assigns each residue a Shannon entropy based on a graph-derived map of accessible substates, providing a continuous measure of structural complexity across folded, unfolded, and intrinsically disordered states. In molecular dynamics simulations of the fast-folding gpW protein, the average local entropy exhibits a sharp transition near the melting point. Residue-specific entropy curves cluster into distinct unfolding categories and reveal that the apparent unfolding transition depends on the spatial scale used to describe amino-acid environments. We further show that local entropy captures features that differ markedly from other

SUBMITTER: Senet P 

PROVIDER: S-EPMC12826060 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature