Dynamics-Evolution Correspondence in Protein Structures

The genotype-phenotype mapping of proteins is a fundamental question in structural biology. In this Letter, with the analysis of a large dataset of proteins from hundreds of protein families, we quantitatively demonstrate the correlations between the noise-induced protein dynamics and mutation-induced variations of native structures, indicating the dynamics-evolution correspondence of proteins. Based on the investigations of the linear responses of native proteins, the origin of such a correspondence is elucidated. It is essential that the noise- and mutation-induced deformations of the proteins are restricted on a common low-dimensional subspace, as confirmed from the data. These results suggest an evolutionary mechanism of the proteins gaining both dynamical flexibility and evolutionary structural variability.

Automated summary

In this study, the correlation between noise-induced protein dynamics and mutation-induced variations of native structures was quantitatively demonstrated through the analysis of a large dataset of proteins. The research suggests an evolutionary mechanism where proteins gain dynamical flexibility and evolutionary structural variability by being restricted to a common low-dimensional subspace for noise- and mutation-induced deformations.