Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering†
* Corresponding authors
a Institute for Research in Biomedicine, Parc Científic de Barcelona, Baldiri Reixac, 10, 08028 Barcelona, Spain
b European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, 22603 Hamburg, Germany
E-mail:pau.bernado@irbbarcelona.org,svergun@embl-hamburg.de
Abstract
Small-angle scattering of X-rays (SAXS) is an established method to study the overall structure and structural transitions of biologicalmacromolecules in solution. For foldedproteins, the technique provides three-dimensional low resolution structuresab initio or it can be used to drive rigid-body modeling.SAXS is also a powerful tool for the quantitative analysis of flexible systems, including intrinsically disorderedproteins (IDPs), and is highly complementary to the high resolution methods ofX-ray crystallography andNMR. Here we present the basic principles ofSAXS and review the main approaches to the characterization of IDPs and flexible multidomainproteins usingSAXS. Together with the standard approaches based on the analysis of overall parameters, a recently developed Ensemble Optimization Method (EOM) is now available. The latter method allows for the co-existence of multipleprotein conformations in solution compatible with the scattering data. Analysis of the selected ensembles provides quantitative information about flexibility and also offers insights into structural features. Examples of the use ofSAXS and combined approaches withNMR,X-ray crystallography, and computational methods to characterize completely or partially disorderedproteins are presented.
- This article is part of the themed collection:Intrinsically Disordered Proteins
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- Article type
- Review Article
- Submitted
- 04 Jul 2011
- Accepted
- 02 Sep 2011
- First published
- 22 Sep 2011
Permissions
Structural analysis of intrinsically disorderedproteins by small-angle X-ray scattering
P. Bernadó and D. I. Svergun,Mol. BioSyst., 2012, 8, 151DOI: 10.1039/C1MB05275F
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