Predicting Local Structural Changes that Results from Point Mutations

Point mutations are frequently used to explore the structure and/or function of proteins. The ability to predict the structural effects of point mutations would make the planning of such experiments more reliable. We have now derived a set of detailed predictive rules based on the comparison of crystal structures of point mutants and wild types in 83 cases. Despite the surprising simplicity of these rules, they describe well the conformational changes in 85% of all point mutant structures available at present.