Predicting protein–DNA binding free energy change upon missense mutations using modified MM/PBSA approach: SAMPDI webserver

摘要

MotivationProtein–DNA interactions are essential for regulating many cellular processes, such as transcription, replication, recombination and translation. Amino acid mutations occurring in DNA-binding proteins have profound effects on protein–DNA binding and are linked with many diseases. Hence, accurate and fast predictions of the effects of mutations on protein–DNA binding affinity are essential for understanding disease-causing mechanisms and guiding plausible treatments.