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

- Despite the absence of permanent structure, IDPs perform crucial functions in biology.
- Structural studies of IDPs require the combination of SAS with computation.
- Ensemble methods provide novel structural information for IDPs in solution.
- Hybrid methods are necessary to characterize flexible and polydisperse systems.

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.

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