QENS spectra of myoglobin in solution to be used with the analysis codes deposited under 10.5281/zenodo.7058345
Authors/Creators
- 1. Jülich Centre for Neutron Science (JCNS-1) and Institute of Biological Information Processing (IBI-8), Forschungszentrum Jülich GmbH, 52425 Jülich, Germ
- 2. ISIS Facility, Rutherford Appleton Laboratory, Didcot OX11 0QX, UK
- 3. Institut Laue-Langevin, 71 Avenue des Martyrs, CS 20156, 38042 Grenoble Cedex 9, France
- 1. Centre de Biophysique Moléculaire, CNRS and Univ. d'Orléans, Rue Charles Sadron, 45071 Orléans, France
Description
Quasielastic Neutron Scattering spectra of myoglobin in solution recorded on the IN5 spectrometer at the Institut Laue-Langevin in Grenoble, France. The data sets are to be used with the analysis codes deposited under DOI:10.5281/zenodo.7058345, which are in turn related to the publication A. Hassani, A. M. Stadler, and G.R. Kneller, Quasi-analytical resolution-correction of elastic neutron scattering from proteins, to appear in the Journal of Chemical Physics (DOI:10.1063/5.0103960).
The data can be freely used, citing properly the reference concerning the original data, A. M. Stadler, F. Demmel, J. Ollivier, and T. Seydel, Picosecond to Nanosecond Dynamics Provide a Source of Conformational Entropy for Protein Folding. Phys. Chem. Chem. Phys., 18(31):21527–21538, 2016 (DOI: 10.1039/c6cp04146a).
Files
IN5_apoMb-2-SolventSubtracted-HDF5.zip
Files
(3.3 MB)
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Additional details
References
- A. M. Stadler, F. Demmel, J. Ollivier, and T. Seydel. Picosecond to Nanosecond Dynamics Provide a Source of Conformational Entropy for Protein Folding. Phys. Chem. Chem. Phys., 18(31):21527–21538, 2016 (DOI: 10.1039/c6cp04146a)
- A. Hassani, A. M. Stadler, and G.R. Kneller, Quasi-analytical resolution-correction of elastic neutron scattering from proteins, to appear in the Journal of Chemical Physics (DOI:10.1063/5.0103960)