Input proteins with mutations

Predict stability effects of mutations on protein folding and interactions

Use the format protein.mutation (example):
or upload file
Warning: because some of the selected proteins are not human, the calculations can take up to several hours.
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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.
Final ΔΔG
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.
Seq iden:
Model score:
ELASPIC2 (EL2) score: