Critical Fluctuations in the Native State of Proteins

Based on protein structural ensembles determined by nuclear magnetic resonance, we study the position fluctuations of residues by calculating distance-dependent correlations and conducting finite-size scaling analysis. The fluctuations exhibit high susceptibility and long-range correlations up to th...

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Bibliographic Details
Published in:Physical review letters 2017-02, Vol.118 (8), p.088102-088102, Article 088102
Main Authors: Tang, Qian-Yuan, Zhang, Yang-Yang, Wang, Jun, Wang, Wei, Chialvo, Dante R
Format: Article
Language:English
Subjects:
Correlation
Correlation analysis
Fluctuation
Magnetic permeability
Mathematical analysis
Proteins
Residues
Scaling
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Summary:Based on protein structural ensembles determined by nuclear magnetic resonance, we study the position fluctuations of residues by calculating distance-dependent correlations and conducting finite-size scaling analysis. The fluctuations exhibit high susceptibility and long-range correlations up to the protein sizes. The scaling relations between the correlations or susceptibility and protein sizes resemble those in other physical and biological systems near their critical points. These results indicate that, at the native states, motions of each residue are felt by every other one in the protein. We also find that proteins with larger susceptibility are more frequently observed in nature. Overall, our results suggest that the protein's native state is critical.
ISSN:0031-9007
1079-7114
DOI:10.1103/PhysRevLett.118.088102