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

Tiago N. Cordeiro; Fátima Herranz-Trillo; Annika Urbanek; Alejandro Estaña; Juan Cortés; Nathalie Sibille; Pau Bernadó

doi:10.1016/j.sbi.2016.10.011

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

Tiago N. Cordeiro, Fátima Herranz-Trillo, Annika Urbanek, Alejandro Estaña, Juan Cortés, Nathalie Sibille, Pau Bernadó

X-ray and Neutron Science

42 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Current Opinion in Structural Biology
Vol/bind	42
Sider (fra-til)	15-23
Antal sider	9
ISSN	0959-440X
DOI	https://doi.org/10.1016/j.sbi.2016.10.011
Status	Udgivet - 2017

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10.1016/j.sbi.2016.10.011

1-s2.0-S0959440X16301749-mainForlagets udgivne version, 972 KB

http://arxiv.org/pdf/1611.02016Licens: Andet

Citationsformater

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AU - Cordeiro, Tiago N.

AU - Herranz-Trillo, Fátima

AU - Urbanek, Annika

AU - Estaña, Alejandro

AU - Cortés, Juan

AU - Sibille, Nathalie

AU - Bernadó, Pau

PY - 2017

Y1 - 2017

N2 - 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.

AB - 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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VL - 42

SP - 15

EP - 23

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

ER -

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

Abstract

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