Structural Information on Bacterial Amyloid and Amyloid-DNA Complex Obtained by Small-Angle Neutron or X-Ray Scattering
- PMID: 35951294
- DOI: 10.1007/978-1-0716-2529-3_6
Structural Information on Bacterial Amyloid and Amyloid-DNA Complex Obtained by Small-Angle Neutron or X-Ray Scattering
Abstract
Small-angle scattering is a powerful technique to obtain structural information on biomacromolecules in aqueous solution at the sub-nanometer and nanometer length scales. It provides the sizes and overall shapes of the scattering particles. While small-angle X-ray scattering (SAXS) has often been used for structural analysis of a single-component system, small-angle neutron scattering (SANS) has been used to reveal the internal organization of a multicomponent system such as protein-protein and protein-DNA complexes. This is due to the fact that the neutron scattering length is largely different between hydrogen and deuterium, and thus it allows to make a specific component in complexes "invisible" to neutrons by changing the H2O/D2O ratio in the solvent with or without molecular deuteration. In this chapter, we describe a method to characterize the biomolecular structures using SANS and SAXS, in particular, focusing on fibrillar proteins such as bacterial amyloids and their complexes with nucleic acids.
Keywords: Bacterial amyloid; Protein-DNA complex; Small-angle X-ray scattering; Small-angle neutron scattering; Structural analysis.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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References
-
- Koch MH, Vachette P, Svergun DI (2003) Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution. Q Rev Biophys 36:147–227 - DOI
-
- Mertens HD, Svergun DI (2010) Structural characterization of proteins and complexes using small-angle X-ray solution scattering. J Struct Biol 172:128–141. https://doi.org/10.1016/j.jsb.2010.06.012 - DOI - PubMed
-
- Gabel F (2017) Applications of SANS to study membrane protein systems. Adv Exp Med Biol 1009:201–214. https://doi.org/10.1007/978-981-10-6038-0_12 - DOI - PubMed
-
- Lapinaite A, Carlomagno T, Gabel F (2020) Small-angle neutron scattering of RNA-protein complexes. Methods Mol Biol 2113:165–188. https://doi.org/10.1007/978-1-0716-0278-2_13 - DOI - PubMed
-
- Thiyagarajan P, Burkoth TS, Urban V et al (2000) pH dependent self assembly of β-amyloid(10-35) and β-amyloid(10-35)-PEG3000. J Appl Crystallogr 33:535–539. https://doi.org/10.1107/S0021889899014387 - DOI
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