Abstract

This chapter describes protein interactions, as one of the major challenges in computational/molecular biology. Predicting the binding interfaces, binding strengths, kinetics, and sensitivity to environmental change or to mutations are all important for understanding the functions of living systems. In recent years, rapid progress has been shown for understanding and predicting the binding site residues and binding specificities in protein–protein, protein–nucleic acid, and protein–ligand complexes. These studies pave ways to understand several functions. Protein–protein interactions play a key role in many biological processes, such as signal transduction, gene expression and control, and antibody–antigen complex. Several investigations have been carried out to understand the details of interactions between the residues at protein–protein interface and the identification of binding sites. The accumulation of data on protein–protein interactions helps in understanding the role of different factors for the specificity of protein–protein interactions and predicting the binding sites. It aims to integrate the diverse body of experimental evidence on protein–protein interactions into a single, easily accessible online database. This database is a resource of genomic and proteomic information and providing an integrated view of sequence, structure, function, and protein networks in health and disease. It has been shown that the surfaces involved in protein–protein contacts differ from the rest of the subunit interface.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call