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Updated: Jun 25, 2026
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Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
Published on: April 25, 2025
On the relation between residue flexibility and local solvent accessibility in proteins
Hua Zhang1, Tuo Zhang, Ke Chen
1Nankai University, Tianjin, People's Republic of China. zerohua@gmail.com
Proteins
|March 11, 2009
Summary
Residue flexibility, measured by B-factor, is significantly influenced by neighboring solvent accessibility. Incorporating local relative solvent accessibility (RSA) improves predictions of protein flexibility and disorder.
Area of Science:
- Structural biology
- Computational biology
- Biophysics
Background:
- Protein flexibility is crucial for function.
- Relative solvent accessibility (RSA) is a key structural property.
- Understanding the interplay between flexibility and solvent accessibility is vital.
Purpose of the Study:
- To investigate the relationship between residue flexibility (B-factor) and local solvent accessibility.
- To assess the impact of neighboring residue accessibility on B-factor.
- To explore the utility of RSA in predicting protein disorder.
Main Methods:
- Analysis of B-factor and RSA correlations.
- Inclusion of local RSA in prediction models.
- Comparison with existing prediction approaches.
- Validation using case studies.
Main Results:
- Local RSA strongly correlates with B-factor, outperforming depth-based measures.
- Flexibility-exposure correlation index links amino acid properties to folding stability.
- Predicted RSA effectively distinguishes ordered from disordered residues.
- Models based on local RSA show improved B-factor and disorder prediction.
Conclusions:
- Local solvent accessibility is a critical determinant of protein residue flexibility.
- Predicted RSA can serve as a valuable tool for disorder prediction.
- This study provides insights into the structure-flexibility-function relationship.
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