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High-resolution Neutron Spectroscopy to Study Picosecond-nanosecond Dynamics of Proteins and Hydration Water

dc.rights.licenseopenen_US
dc.contributor.authorPOUNOT, Kevin
dc.contributor.authorAPPEL, Markus
dc.contributor.authorBECK, Christian
dc.contributor.authorWEIK, Martin
dc.contributor.authorSCHIRO, Giorgio
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorFICHOU, Yann
dc.contributor.authorSEYDEL, Tilo
dc.contributor.authorSCHREIBER, Frank
dc.date.accessioned2023-05-24T11:40:07Z
dc.date.available2023-05-24T11:40:07Z
dc.date.issued2022-04-28
dc.identifier.issn1940-087Xen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182305
dc.description.abstractEnNeutron scattering offers the possibility to probe the dynamics within samples for a wide range of energies in a nondestructive manner and without labeling other than deuterium. In particular, neutron backscattering spectroscopy records the scattering signals at multiple scattering angles simultaneously and is well suited to study the dynamics of biological systems on the ps-ns timescale. By employing D2O-and possibly deuterated buffer components-the method allows monitoring of both center-of-mass diffusion and backbone and side-chain motions (internal dynamics) of proteins in liquid state. Additionally, hydration water dynamics can be studied by employing powders of perdeuterated proteins hydrated with H2O. This paper presents the workflow employed on the instrument IN16B at the Institut Laue-Langevin (ILL) to investigate protein and hydration water dynamics. The preparation of solution samples and hydrated protein powder samples using vapor exchange is explained. The data analysis procedure for both protein and hydration water dynamics is described for different types of datasets (quasielastic spectra or fixed-window scans) that can be obtained on a neutron backscattering spectrometer. The method is illustrated with two studies involving amyloid proteins. The aggregation of lysozyme into µm sized spherical aggregates-denoted particulates-is shown to occur in a one-step process on the space and time range probed on IN16B, while the internal dynamics remains unchanged. Further, the dynamics of hydration water of tau was studied on hydrated powders of perdeuterated protein. It is shown that translational motions of water are activated upon the formation of amyloid fibers. Finally, critical steps in the protocol are discussed as to how neutron scattering is positioned regarding the study of dynamics with respect to other experimental biophysical methods.
dc.language.isoENen_US
dc.title.enHigh-resolution Neutron Spectroscopy to Study Picosecond-nanosecond Dynamics of Proteins and Hydration Water
dc.typeArticle de revueen_US
dc.identifier.doi10.3791/63664en_US
dc.subject.halChimie/Matériauxen_US
dc.description.sponsorshipEuropeEuropeen_US
dc.description.sponsorshipEuropeDeuteration consortiumen_US
bordeaux.journalJoVE (Journal of Visualized Experiments)en_US
bordeaux.hal.laboratoriesCBMN : Chimie & de Biologie des Membranes & des Nano-objets - UMR 5248en_US
bordeaux.issue182en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.exportfalse
dc.rights.ccPas de Licence CCen_US
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