Small-angle scattering studies of intrinsically disordered proteins and their complexes

TL;DR

This review discusses recent advances in using Small-Angle Scattering (SAS) to study intrinsically disordered proteins and their complexes, highlighting new computational tools and integration with other structural methods.

Contribution

It provides an overview of recent methodological developments and challenges in applying SAS to characterize disordered proteins and their flexible complexes.

Findings

SAS effectively probes size and shape of disordered proteins.

Computational tools enhance interpretation of low-resolution SAS data.

Integration with other methods improves structural insights.

Abstract

Intrinsically Disordered Proteins (IDPs) perform a broad range of biological functions. Their relevance has motivated intense research activity seeking to characterize their sequence/structure/function relationships. However, the conformational plasticity of these molecules hampers the application of traditional structural approaches, and new tools and concepts are being developed to address the challenges they pose. Small-Angle Scattering (SAS) is a structural biology technique that probes the size and shape of disordered proteins and their complexes with other biomolecules. The low-resolution nature of SAS can be compensated with specially designed computational tools and its combined interpretation with complementary structural information. In this review, we describe recent advances in the application of SAS to disordered proteins and highly flexible complexes and discuss current challenges.