A Novel Method for Protein-Protein Interface Analysis Using Sonification

Auditory inspection reduces analytical subjectivity through concrete musical parameters. Here, it is applied to oligomerically varied protein-protein interfaces (PPIs) in a harmony-based sonification method. Amino acids in the PPI bonded contacts for homo- and hetero- di/tri/tetramers were grouped using four qualitative systems. PPI hydrogen bonds and salt bridges were examined to determine groups' bonded interaction frequencies, compared using the chi-squared test of independence. Highly significant p-values (<<0.05) for homo- and hetero-oligomers in all systems' oligomeric states strongly suggested that bonded interactions' frequencies differ. These frequencies were successfully sonified using variations in consonance, waveform, chord structure, and pitch.