Experimental Methods to Study Intrinsically Disordered Proteins

Authors

• Niharika Nag, North-Eastern Hill University
• Purna Bahadur Chetri, North-Eastern Hill University
• Vladimir N. Uversky, University of South FloridaFollow
• Rajanish Giri, Indian Institute of Technology Mandi
• Timir Tripathi, North-Eastern Hill University

Document Type

Book Chapter

Publication Date

2022

Keywords

Intrinsically Disordered Proteins, Intrinsically Disordered Regions, Hydrophobicity, Structural Analysis, Binding Partners, Fluorescence, Interaction, Dynamics, Conformation

Digital Object Identifier (DOI)

https://doi.org/10.1016/B978-0-323-90264-9.00031-3

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.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Experimental Methods to Study Intrinsically Disordered Proteins, in T. Tripathi & V. K. Dubey (Eds.), Advances in Protein Molecular and Structural Biology Methods, Academic Press, p. 505-533

Scholar Commons Citation

Nag, Niharika; Chetri, Purna Bahadur; Uversky, Vladimir N.; Giri, Rajanish; and Tripathi, Timir, "Experimental Methods to Study Intrinsically Disordered Proteins" (2022). Molecular Medicine Faculty Publications. 1139.
https://digitalcommons.usf.edu/mme_facpub/1139