Rationalization of protein side chain flexibility and ligand bind | 33433
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

+44 1223 790975

Rationalization of protein side chain flexibility and ligand binding based on cooperative interaction networks

6th International Conference on Structural Biology

August 22-23, 2016 New Orleans, USA

Neil R Taylor

Desert Scientific Software, Australia

Posters & Accepted Abstracts: J Proteomics Bioinform

Abstract :

Network concepts have been widely applied in structure biology research to help the understanding of protein structure and function. Our research approach is based on applying small world network concepts to ligand-protein complexes, using atomic level representation of favorable close contacts, focusing on local cooperativity. Specifically, we believe that there are patterns of networked interactions, currently overlooked using traditional additive methods that play important roles in ligand-protein binding. We believe small world network concepts are keys in identifying these patterns because although they may involve weakly favorable contacts, they can be highly stabilizing. To demonstrate the effectiveness of these novel small world network concepts we show complexes involving Aurora A kinase, and how the visualization of key interaction networks supports the rationalization of binding site hot-spots and residue mobility. To further explore the local cooperativity of interacting residues in protein crystal structure data, we introduce new and novel methods for the fast searching of networked interactions.

Biography :