Quick search Find article
Quick search
Find article

Character and evolution of protein–protein interfaces

Ivica Reš and Olivier Lichtarge

Show affiliations


Protein–protein interactions create the macromolecular assemblies and sequential signaling pathways essential for cell function. Their number far exceeds the number of proteins themselves and their experimental characterization, while improving, remains relatively slow. For these reasons, novel computational methods have important roles to play in understanding the physical basis of protein interactions, and in constraining the molecular basis of their specificity. This paper discusses methods based on multiple sequence alignments of protein homologues and phylogenetic trees.


PACS

87.15.K- Molecular interactions; membrane-protein interactions

87.14.E- Proteins

87.15.Cc Folding: thermodynamics, statistical mechanics, models, and pathways

87.16.Ka Filaments, microtubules, their networks, and supramolecular assemblies

87.16.Xa Signal transduction and intracellular signaling

Subjects

Biological physics

Dates

Issue 2 (June 2005)

Received 7 March 2005, accepted for publication 9 May 2005

Published 27 May 2005

 
The point on the specificity versus sensitivity plot for the prediction of protein–protein interaction sites signifying an accuracy of 64%.


View by subject




Export








Please login to access our web services, or create an account if you don't yet have one.

You must have cookies enabled in your web browser to be able to login.

Username
Password

Forgotten your password? Get a new one here.