The DOI matches its Crossref record; 139 of the 139 references it cites were found in a registry or an index.
Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering
Open accessAbstract
Small-angle scattering of X-rays (SAXS) is an established method to study the overall structure and structural transitions of biological macromolecules in solution. For folded proteins, the technique provides three-dimensional low resolution structures ab 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 disordered proteins (IDPs), and is highly complementary to the high resolution methods of X-ray crystallography and NMR. Here we present the basic principles of SAXS and review the main approaches to the characterization of IDPs and flexible multidomain proteins using SAXS. 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 multiple protein 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 of SAXS and combined approaches with NMR, X-ray crystallography, and computational methods to characterize completely or partially disordered proteins are presented.
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Relation between single-molecule properties and phase behavior of intrinsically disordered proteins
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Metadata
- Authors
- Bernadó, P., & Svergun, D. I.
- Venue
- Molecular BioSystems
- Publisher
- Oxford University Press (OUP)
- Published
- 2011-09-22
- Volume
- 8
- Issue
- 1
- Pages
- 151-167
- ISSN
- 1742-2051 (ISSN-L)
- 1742-206X
- OpenAlex
- W2101137168
- Cited by
- 347
- References
- 139
- FWCI
- 8.35
- Type
- journal article
- Language
- en
- Open access
- green
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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