Input proteins with mutations
Predict stability effects of mutations on protein folding and interactions
Use the format
Warning: because some of the selected proteins are not human, the calculations can take up to several hours.
Your email address (optional):
Because ELASPIC uses structures of protein domains to predict stability/affinity effects, the mutation has to fall within domain boundries.
For more information about the mechanisms of ELASPIC, see
the published paper
The final Gibbs free energy change (ΔΔG) in kcal/mol is predicted using more than 70 sequential, molecular, and energetic features.
For more information see
the original publication
Final ΔΔG (
© 2016 –
University of Toronto