ProTSPoM
ProTSPoM predicts alterations in Gibbs free energy caused by missense mutations to evaluate effects on protein stability by integrating residue properties, fold-level attributes, environmental compatibility, and evolutionary information using Random Forest and Gradient Boosted Regressors.
Key Features:
- Machine learning models: Employs Random Forest Regressors and Gradient Boosted Regressors for regression of Gibbs free energy changes due to missense mutations.
- Input feature types: Integrates residue properties, fold-level attributes, environmental compatibility metrics, and evolutionary information as predictive features.
- Prediction target: Predicts alterations in Gibbs free energy (stability changes) resulting from single amino-acid substitutions.
- Benchmark performance: Reports Pearson correlation coefficients of 0.82 for S350 and 0.88 for p53 with root-mean-squared-errors of 0.92 kcal/mol for S350 and 1.06 kcal/mol for p53.
Scientific Applications:
- p53 protein analysis: Identifies missense mutations that affect the structural integrity and DNA binding affinity of p53.
Methodology:
Uses Random Forest and Gradient Boosted Regressors to integrate residue properties, fold-level attributes, environmental compatibility, and evolutionary information to predict Gibbs free energy changes from missense mutations.
Topics
Details
- Added:
- 1/18/2021
- Last Updated:
- 1/29/2021
Operations
Publications
Banerjee A, Mitra P. Estimating the Effect of Single-Point Mutations on Protein Thermodynamic Stability and Analyzing the Mutation Landscape of the p53 Protein. Journal of Chemical Information and Modeling. 2020;60(6):3315-3323. doi:10.1021/acs.jcim.0c00256. PMID:32401507.