Localization of Energetic Frustration in Proteins

TL;DR

This paper introduces a heuristic method to quantify local energetic frustration in proteins, aiding in identifying stable cores and functionally important regions like binding sites.

Contribution

The paper presents a novel heuristic approach for quantifying local energetic frustration in proteins, enhancing the understanding of structure-function relationships.

Findings

Minimally frustrated regions correspond to stable folding cores.

Highly frustrated sites often indicate functional regions such as binding or active sites.

Method visualizes energetic conflicts in protein structures.

Abstract

We present a detailed heuristic method to quantify the degree of local energetic frustration manifested by protein molecules. Current applications are realized in computational experiments where a protein structure is visualized highlighting the energetic conflicts or the concordance of the local interactions in that structure. Minimally frustrated linkages highlight the stable folding core of the molecule. Sites of high local frustration, in contrast, often indicate functionally relevant regions such as binding, active or allosteric sites.