Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequence.

doi:10.1006/jmbi.1997.1237

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Article

Predicting protein stability changes upon mutation using database-derived potentials: solvent accessibility determines the importance of local versus non-local interactions along the sequence.

Journal of molecular biology - 19 Sept 1997

Gilis D, Rooman M

Abstract excerpt

For 238 mutations of residues totally or partially buried in the protein core, we estimate the folding free energy changes upon mutation using database-derived potentials and correlate them with the experimentally measured ones. Several potentials are tested, representing different kinds of inter...

Topics

Animals
Enzyme Stability
Humans
Mutation
Protein Folding
Protein Structure, Secondary
Proteins
Solvents
Thermodynamics

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