Related Experiment Video
Updated: Aug 25, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
Perspectives on evolutionary and functional importance of intrinsically disordered proteins
Tanuj Handa1, Debanjan Kundu1, Vikash Kumar Dubey1
1School of Biochemical Engineering, Indian Institute of Technology BHU, Varanasi, UP 221005, India.
Abstract:
Structural biology of proteins emphasises that proteins ought to have an ordered structure to perform their biological role optimally. The over-reliance on the ordered structure of proteins is now slowly shifting towards a more comprehensive discussion platform. Intrinsically disordered proteins (IDPs) and intrinsically disordered protein regions (IDPRs) are gaining momentum in protein structural biology as we update ourselves with evolutionary traits and functional importance in various organisms. The evolution and functional significance of this diverse class of protein conformations are based on sequence exhibition, structural attainment, and interactions with their immediate surroundings. In this review, we emphasise the evolutionary status of disordered proteins and correlate their functional importance in the physiology of specific organisms. We aim to close this review by establishing a positive correlation between IDPs and their importance in human health and future medicine. Establishing firm roles of IDPs and IDPRs with extensive research will help expand the field of structural biology, helping us understand the fundamentals of protein folding and misfolding, associated diseases and drug design.
More Related Videos
05:13Author Spotlight: Unlocking the World of Intrinsically Disordered Regions with Cellular Sensing and Responses
Published on: January 12, 2024
07:24Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
Related Concept Videos
Intrinsically Disordered Proteins
Protein Folding
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
Molecular Chaperones and Protein Folding
The...
Protein-protein Interfaces