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.

Details

Title
High-resolution neutron spectroscopy on protein solution samples
Author
Grimaldo, Marco; Roosen-Runge, Felix; Jalarvo, Niina; Zamponi, Michaela; Zanini, Fabio; Hennig, Marcus; Zhang, Fajun; Schreiber, Frank; Seydel, Tilo
Section
QENS 2014
Publication year
2015
Publication date
2015
Publisher
EDP Sciences
ISSN
21016275
e-ISSN
2100014X
Source type
Conference Paper
Language of publication
English
ProQuest document ID
1762721674
Copyright
© 2015. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and conditions, you may use this content in accordance with the terms of the License.