ResiCon: a method for the identification of dynamic domains, hinges and interfacial regions in proteins

Maciej Dziubinski, Pawel Daniluk, Bogdan Lesyng

Abstract: Structure of most proteins is flexible. Identification and analysis of intramolecular motions is a complex problem. Breaking a structure into relatively rigid parts, the so-called dynamic domains, may help comprehend the complexity of protein’s mobility. We propose a new approach called ResiCon (Residue Contacts analysis), which performs this task by applying a data-mining analysis of an ensemble of protein configurations and recognizes dynamic domains, hinges and interfacial regions, by considering contacts between residues.