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DOI: 10.3791/63664-v
Kevin Pounot1,2, Markus Appel2, Christian Beck1,2, Martin Weik3, Giorgio Schirò3, Yann Fichou4, Tilo Seydel2, Frank Schreiber1
1Institut für Angewandte Physik,Universität Tübingen, 2Institut Max von Laue - Paul Langevin (ILL), 3Institut de Biologie Structurale,Université Grenoble Alpes, 4Institut Européen de Chimie et Biologie, Bordeaux INP, Chimie et Biologie des Membranes et des Nanoobjets (CBMN),Université de Bordeaux
Neutron backscattering spectroscopy offers a nondestructive and label-free access to the ps-ns dynamics of proteins and their hydration water. The workflow is presented with two studies on amyloid proteins: on the time-resolved dynamics of lysozyme during aggregation and on the hydration water dynamics of tau upon fiber formation.
Neutron backscatterings measures global diffusion and internal dynamics of proteins and hydration water without radiation damage. Neutron spectroscopy simultaneously accesses spatial and time correlations on a molecular level. In soft matter and biological materials, it's particularly interesting to obtain indirect information on local order on these long range disorder systems.
So neutron backscattering can be used to study dynamics in biology, chemistry, or material sense. Another strong field is energy, with studies, for instance, on batteries and fuel cells. Neutron backscattering has been used successfully to study the molecular dynamics of proteins involved in neurodegenerative diseases such as Alzheimer's and Parkinson's.
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