We've updated our Privacy Policy to make it clearer how we use your personal data.

We use cookies to provide you with a better experience. You can read our Cookie Policy here.


Predicting Protein-Protein Interface Residues Using Local Surface Structural Similarity

Want a FREE PDF version of This News Story?

Complete the form below and we will email you a PDF version of "Predicting Protein-Protein Interface Residues Using Local Surface Structural Similarity"

Technology Networks Ltd. needs the contact information you provide to us to contact you about our products and services. You may unsubscribe from these communications at any time. For information on how to unsubscribe, as well as our privacy practices and commitment to protecting your privacy, check out our Privacy Policy

Read time:

In the past decade, significant efforts have been devoted to characterization as well as discovery of these interactions both in silico and in vivo. Of particular interest is the identification of the amino acid residues that participate in protein-protein interactions because of its importance in elucidation of mechanisms that underlay biological function and rational drug design (among other applications). However, experimental determination of interface residues is expensive, labor intensive, and time consuming. Hence, there is an urgent need for computational methods for reliably identifying from the sequence or structure of a query protein, the subset of residues that are likely to be involved in the interaction of that protein with one or more other proteins.

This article is published online in BMC Bioinformatics and is free to access.