Recognition of Interaction Interface Residues in Low-Resolution Structures of Protein Assemblies Solely from the Positions of Cα Atoms
2009

Identifying Protein Residues from Cα Positions

Sample size: 1100 publication 10 minutes Evidence: high

Author Information

Author(s): Gadkari Rupali A., Varughese Deepthi, Srinivasan N.

Primary Institution: Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India

Hypothesis

Can we accurately identify solvent exposed and buried residues in proteins using only the positions of Cα atoms?

Conclusion

The method developed can accurately identify buried and exposed residues from Cα positions with high sensitivity and specificity.

Supporting Evidence

  • The method achieved an accuracy of 84% in identifying buried residues.
  • Sensitivity for buried residues was found to be 89%, while specificity was 67%.
  • For interface residues, accuracy reached 94%, with sensitivity of 70% and specificity of 58%.
  • The approach is particularly useful for analyzing low-resolution protein structures.

Takeaway

Scientists found a way to tell which parts of proteins are hidden or exposed just by looking at certain points on them, which helps understand how proteins work together.

Methodology

The study used a method to analyze Cα atom positions to identify solvent exposed and buried residues, and extended this to recognize protein-protein interface residues.

Limitations

The method relies solely on Cα positions, which may not capture all structural details.

Statistical Information

P-Value

p<0.05

Statistical Significance

p<0.05

Digital Object Identifier (DOI)

10.1371/journal.pone.0004476

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