Abstract
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.
Highlights
Phenotypic states of all living systems are shaped through dynamics, which are changed through evolution
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
Summary
Phenotypic states of all living systems are shaped through dynamics, which are changed through evolution. 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. The conformational dynamics are subjected to thermal noises, which can trigger functional motions [9–13], whereas the mutations in the sequences may lead to deformations in their native structure, resulting in changes in the equilibrium dynamics of the proteins.
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