Chapter 31 - Experimental methods to study intrinsically disordered proteins

Abstract

Although under physiological conditions, intrinsically disordered proteins (IDPs) fail to form a definite 3D structure and instead exist as ensembles of conformations, they perform critical biological functions. The intrinsically disordered regions (IDPRs) are involved in molecular recognition, cellular regulation, and signaling via binding to multiple partners with high-specificity and low-affinity interactions. Understanding the structural and conformational properties of IDPs is critical to characterize the diseases associated with them and design better inhibitors. In recent years, several techniques emerged that could provide information on the conformation, dynamics, and interactions of the IDPs. In this chapter, we review the experimental methods to characterize the IDPs and IDPRs.