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

Tiago Cordeiro 1 Fatima Herranz-Trillo 2, 1 Annika Urbanek 1 Alejandro Estaña 1, 3 Juan Cortés 3 Nathalie Sibille 1 Pau Bernadó 1
1 CBS - Centre de Biochimie Structurale [Montpellier]
2 Department of Drug Design and Pharmacology, University of Copenhagen
3 LAAS-RIS - Équipe Robotique et InteractionS
LAAS - Laboratoire d'analyse et d'architecture des systèmes [Toulouse]
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.
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Current Opinion in Structural Biology, Elsevier, 2017, 42, pp.15 - 23. 〈10.1016/j.sbi.2016.10.011〉
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Tiago Cordeiro, Fatima Herranz-Trillo, Annika Urbanek, Alejandro Estaña, Juan Cortés, et al.. Small-angle scattering studies of intrinsically disordered proteins and their complexes. Current Opinion in Structural Biology, Elsevier, 2017, 42, pp.15 - 23. 〈10.1016/j.sbi.2016.10.011〉. 〈hal-01391541〉

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