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Effective use of sequence correlation and conservation in fold recognition
1Protein Design Group, CNB-CSIC, Cantoblanco, Madrid, E-28049, Spain.
Journal of Molecular Biology
|November 5, 1999
Summary
Analyzing protein families reveals sequence conservation and correlation can detect misfolded proteins. Combining these with polarity significantly improves protein fold recognition in threading methods.
Area of Science:
- Bioinformatics
- Computational Biology
- Protein Science
Background:
- Protein families offer insights through sequence conservation and correlation analysis.
- Sequence conservation reflects evolutionary pressure on protein function.
- Sequence correlation relates to adjustments maintaining protein stability.
Purpose of the Study:
- To investigate the utility of sequence conservation and correlation in identifying incorrectly folded proteins.
- To enhance protein threading methods using sequence-based properties.
Main Methods:
- Analysis of multiple sequence alignments to derive sequence conservation and correlation.
- Development of a scoring system combining conservation, correlation, and polarity.
- Evaluation of protein models using a threading approach based on residue proximity.
Main Results:
- Sequence conservation and correlation alone were effective in detecting misfolded proteins.
- A combined approach using conservation, correlation, and polarity achieved near-perfect discrimination.
- Protein threading fold recognition capacity improved nearly fourfold with the proposed scoring method.
Conclusions:
- Sequence-based properties are powerful indicators for protein folding accuracy.
- Integrating conservation, correlation, and polarity enhances protein structure prediction and fold recognition.