Functionally important residues from graph analysis of coevolved dynamic couplings.

ABSTRACT: The relationship between protein dynamics and function is essential for understanding biological processes and developing effective therapeutics. Functional sites within proteins are critical for activities such as substrate binding, catalysis, and structural changes. Existing computational methods for the predictions of functional residues are trained on sequence, structural, and experimental data, but they do not explicitly model the influence of evolution on protein dynamics. This overlooked contribution is essential as it is known that evolution can fine-tune protein dynamics through compensatory mutations either to improve the proteins' performance or diversify its function while maintaining the same structural scaffold. To model this critical contribution, we introduce DyNoPy, a comp

SUBMITTER: Xu M 

PROVIDER: S-EPMC11952748 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature