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Updated: Sep 1, 2025

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
Structural Information on Bacterial Amyloid and Amyloid-DNA Complex Obtained by Small-Angle Neutron or X-Ray
Tatsuhito Matsuo1,2,3, Véronique Arluison4,5, Frank Wien6
1Univ. Grenoble Alpes, CNRS, LiPhy, Grenoble, France. matsuo@ill.fr.
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.
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