Applications of Bioinformatics and Experimental Methods to Intrinsic Disorder-Based Protein-Protein Interactions

Abstract

Proteins are important to the organisms and they control biochemical pathways within the cell. Each protein or group of proteins are responsible for various functions needed to maintain the living cell, including enzymatic catalysis; transporting or storing chemical compounds and energy; hormone regulation of many processes; maintaining structure of tissues and cells; antibody immune response; signal transduction by receptors and signalling proteins etc. The functions of proteins have been long related to their rigid threedimensional (3D) structures in that a protein's biological function depended on its prior folding into a unique 3D structure. However, as it was discovered in recent years, not all biologically functional proteins fold spontaneously into globular structures. Some protein regions or entire proteins lack stable secondary and/or tertiary structures in solution yet possess crucial biological functions, and these disordered regions or proteins are key to understanding many biological processes such as transcriptional regulation, signalling and causes of diseases. In this chapter, we will focus on some basic concepts of intrinsically disordered proteins (IDPs), the recent progress of structural and functional studies of IDP, and the bioinformatics and experimental methods practically used for investigation of IDPs.