2023 review

Illuminating Intrinsically Disordered Proteins with Integrative Structural Biology

[Review of ]. BIOMOLECULES, 13(1).

By: R. Evans n, S. Ramisetty*, P. Kulkarni * & K. Weninger n 

co-author countries: United States of America 🇺🇸
author keywords: intrinsically disordered proteins; integrative structural biology; unfolded; unstructured; flexible; protein function
MeSH headings : Intrinsically Disordered Proteins / chemistry; Signal Transduction; Biology; Protein Conformation
Source: Web Of Science
Added: February 13, 2023

Intense study of intrinsically disordered proteins (IDPs) did not begin in earnest until the late 1990s when a few groups, working independently, convinced the community that these ‘weird’ proteins could have important functions. Over the past two decades, it has become clear that IDPs play critical roles in a multitude of biological phenomena with prominent examples including coordination in signaling hubs, enabling gene regulation, and regulating ion channels, just to name a few. One contributing factor that delayed appreciation of IDP functional significance is the experimental difficulty in characterizing their dynamic conformations. The combined application of multiple methods, termed integrative structural biology, has emerged as an essential approach to understanding IDP phenomena. Here, we review some of the recent applications of the integrative structural biology philosophy to study IDPs.