PRICE (PRotein Interface Conservation and Energetics): a server for the analysis of protein-protein interfaces.

TitlePRICE (PRotein Interface Conservation and Energetics): a server for the analysis of protein-protein interfaces.
Publication TypeJournal Article
Year of Publication2011
AuthorsGuharoy, M., A. Pal, M. Dasgupta, and P. Chakrabarti
JournalJ Struct Funct Genomics
Volume12
Issue1
Pagination33-41
Date Published2011 Mar
ISSN1570-0267
KeywordsComputational Biology, Databases, Protein, Internet, Models, Molecular, Multiprotein Complexes, Protein Interaction Mapping, Proteins, User-Computer Interface
Abstract

Residues in a protein-protein interface that are important for forming and stabilizing the interaction can usually be identified by looking at patterns of evolutionary conservation in groups of homologous proteins and also by the computational identification of binding hotspots. The PRICE (PRotein Interface Conservation and Energetics) server takes the coordinates of a protein-protein complex, dissects the interface into core and rim regions, and calculates (1) the degree of conservation (measured as the sequence entropy), as well as (2) the change in free energy of binding (∆∆G, due to alanine scanning mutagenesis) of interface residues. Results are displayed as color-coded plots and also made available for download. This enables the computational identification of binding hot spots, based on which further experiments can be designed. The method will aid in protein functional prediction by correct assignment of hot regions involved in binding. Consideration of sequence entropies for residues with large ∆∆G values may provide an indication of the biological relevance of the interface. Finally, the results obtained on a test set of alanine mutants has been compared to those obtained using other servers/methods. The PRICE server is a web application available at http://www.boseinst.ernet.in/resources/bioinfo/stag.html.

DOI10.1007/s10969-011-9108-0
Alternate JournalJ. Struct. Funct. Genomics
PubMed ID21519818
Research group: