期刊
PHYSICAL REVIEW LETTERS
卷 127, 期 9, 页码 -出版社
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.127.098103
关键词
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资金
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [17H06386]
- Japanese Society for the Promotion of Science [20H00123]
- Grants-in-Aid for Scientific Research [20H00123, 17H06386] Funding Source: KAKEN
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.
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.
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