Prediction of protein thermodynamic stability changes upon single-site mutations
PoPMuSiC is a tool for the computer-aided design of mutant proteins with controlled thermodynamic stability properties. It evaluates the changes in folding free energy of a given protein or peptide under point mutations, on the basis of the experimental or modeled protein structure.
Three modes are available:
- Systematic: Evaluation of the stability changes resulting from all possible point mutations. Returns a report with the list of the most stabilizing or destabilizing mutations, or of the mutations that do not affect stability.
- Manual: Prediction of the stability changes caused by the point mutations specified by the user.
- File: Prediction of the stability changes caused by a list of mutations specified by the user in an uploaded file.
Prediction of protein thermostability changes upon single-site mutations
HOTMuSiC is a tool for the computer-aided design of mutant proteins with controlled thermal stability properties. It evaluates the changes in melting temperature of a given protein or peptide under point mutations, on the basis of the experimental or modeled protein structure.
Four modes are available:
- Systematic: Evaluation of the stability changes resulting from all possible point mutations. Returns a report with the list of the most stabilizing or destabilizing mutations, or of the mutations that do not affect stability.
- Manual: Prediction of the stability changes caused by the point mutations specified by the user.
- File: Prediction of the stability changes caused by a list of mutations specified by the user in an uploaded file.
- Wild-type Tm: Predictions with improved accuracy are obtained if the Tm of the wild-type protein is known.