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.
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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:
ELASPIC ΔΔG:
ELASPIC2 (EL2) score: