High-resolution neutron spectroscopy on protein solution samples

Marco Grimaldo; Felix Roosen-Runge; Niina Jalarvo; Michaela Zamponi; Fabio Zanini; Marcus Hennig; Fajun Zhang; Frank Schreiber; Tilo Seydel

doi:10.1051/epjconf/20158302005

High-resolution neutron spectroscopy on protein solution samples

Marco Grimaldo, Felix Roosen-Runge, Niina Jalarvo, Michaela Zamponi, Fabio Zanini, Marcus Hennig, Fajun Zhang, Frank Schreiber, Tilo Seydel

Research output: Contribution to journal › Conference article › peer-review

19 Scopus citations

Abstract

Proteins in solution move subject to a complex superposition of global translational and rotational diffusion as well as internal relaxations covering a wide range of time scales. With the advent of new high-flux neutron spectrometers in combination with enhanced analysis frameworks it has become possible to separate these different contributions. We discuss new approaches to the analysis by presenting example spectra and fits from data recorded on the backscattering spectrometers IN16, IN16B, and BASIS on the same protein solution sample. We illustrate the separation of the rotational and translational diffusion contribution, the accurate treatment of the solvent contribution, and the extraction of information on internal fluctuations. We also exemplify the progress made in passing from second- to third-generation backscattering spectrometers.

Original language	English
Article number	02005
Journal	EPJ Web of Conferences
Volume	83
DOIs	https://doi.org/10.1051/epjconf/20158302005
State	Published - Jan 23 2015
Externally published	Yes
Event	11th International Conference on Quasielastic Neutron Scattering, QENS 2014 and 6th International Workshop on Inelastic Neutron Spectrometers, WINS 2014 - Autrans, France Duration: May 11 2014 → May 16 2014

Funding

Funders	Funder number
Deutsche Forschungsgemeinschaft	240526267

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10.1051/epjconf/20158302005

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title = "High-resolution neutron spectroscopy on protein solution samples",

abstract = "Proteins in solution move subject to a complex superposition of global translational and rotational diffusion as well as internal relaxations covering a wide range of time scales. With the advent of new high-flux neutron spectrometers in combination with enhanced analysis frameworks it has become possible to separate these different contributions. We discuss new approaches to the analysis by presenting example spectra and fits from data recorded on the backscattering spectrometers IN16, IN16B, and BASIS on the same protein solution sample. We illustrate the separation of the rotational and translational diffusion contribution, the accurate treatment of the solvent contribution, and the extraction of information on internal fluctuations. We also exemplify the progress made in passing from second- to third-generation backscattering spectrometers.",

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AU - Grimaldo, Marco

AU - Roosen-Runge, Felix

AU - Jalarvo, Niina

AU - Zamponi, Michaela

AU - Zanini, Fabio

AU - Hennig, Marcus

AU - Zhang, Fajun

AU - Schreiber, Frank

AU - Seydel, Tilo

PY - 2015/1/23

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N2 - Proteins in solution move subject to a complex superposition of global translational and rotational diffusion as well as internal relaxations covering a wide range of time scales. With the advent of new high-flux neutron spectrometers in combination with enhanced analysis frameworks it has become possible to separate these different contributions. We discuss new approaches to the analysis by presenting example spectra and fits from data recorded on the backscattering spectrometers IN16, IN16B, and BASIS on the same protein solution sample. We illustrate the separation of the rotational and translational diffusion contribution, the accurate treatment of the solvent contribution, and the extraction of information on internal fluctuations. We also exemplify the progress made in passing from second- to third-generation backscattering spectrometers.

AB - Proteins in solution move subject to a complex superposition of global translational and rotational diffusion as well as internal relaxations covering a wide range of time scales. With the advent of new high-flux neutron spectrometers in combination with enhanced analysis frameworks it has become possible to separate these different contributions. We discuss new approaches to the analysis by presenting example spectra and fits from data recorded on the backscattering spectrometers IN16, IN16B, and BASIS on the same protein solution sample. We illustrate the separation of the rotational and translational diffusion contribution, the accurate treatment of the solvent contribution, and the extraction of information on internal fluctuations. We also exemplify the progress made in passing from second- to third-generation backscattering spectrometers.

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DO - 10.1051/epjconf/20158302005

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SN - 2101-6275

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JO - EPJ Web of Conferences

JF - EPJ Web of Conferences

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Y2 - 11 May 2014 through 16 May 2014

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High-resolution neutron spectroscopy on protein solution samples

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