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

TitleResiCon: a method for the identification of dynamic domains, hinges and interfacial regions in proteins.
Publication TypeJournal Article
Year of Publication2015
AuthorsDziubiński, Maciej, Daniluk Paweł, and Lesyng Bogdan
JournalBioinformatics
Date Published2015 Sep 5
ISSN1367-4811
Abstract<p><b>MOTIVATION: </b>Structure of most proteins is flexible. Indentification and analysis of intramolecular motions is a complex problem. Breaking a structure into relatively rigid parts, 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.</p><p><b>RESULTS: </b>Dynamic domains found by ResiCon are more compact than those identified by two other popular methods: PiSQRD and GeoStaS. The current analysis was carried out using a known reference set of 30 NMR protein structures, as well as MD simulation data of flap opening events in HIV-1 protease. The more detailed analysis of HIV-1 protease dataset shows that ResiCon identified dynamic domains involved in structural changes of functional importance.</p><p><b>AVAILABILITY: </b>The ResiCon server is available at URL: http://dworkowa.imdik.pan.pl/EP/ResiCon CONTACT: pawel@bioexploratorium.pl.</p>
DOI10.1093/bioinformatics/btv525
Alternate JournalBioinformatics
PubMed ID26342233