Universal Principles of Protein Dynamics and Evolution Revealed by Data-Driven Studies

Abstract

Proteins exhibit structural variations due to thermal noise (dynamics) and genetic mutations (evolution). Using extensive protein structure databases, it is observed that native-state dynamics of proteins exhibit long-range correlations, resembling critical points in physical systems, which contribute to significant conformational changes like allosteric regulation. Additionally, data-driven analysis revealed correspondences between protein dynamics and evolution, shedding light on the robustness-plasticity tradeoff of proteins. Furthermore, based on AlphaFold structure predictions, the statistical trends in protein evolution were observed, highlighted by evolutionary dimensionality reduction. These findings underscore the universal principles of biocomplexity and may lead to advancements of protein engineering technologies.