http://www.cnr.it/ontology/cnr/individuo/prodotto/ID4028
A benchmark for protein dynamics: Ribonuclease A measured by neutron scattering in a large wavevector-energy transfer range (Articolo in rivista)
- Type
- Label
- A benchmark for protein dynamics: Ribonuclease A measured by neutron scattering in a large wavevector-energy transfer range (Articolo in rivista) (literal)
- Anno
- 2008-01-01T00:00:00+01:00 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Kathleen Wood; Chiara Caronna; Peter Fouquet ; Wolfgang Haussler;
Francesca Natali; Jacques Ollivier; Andrea Orecchini; Marie Plazanet;
Giuseppe Zaccai (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Institut Laue Langevin, BP 156, 38042 Grenoble Cedex 9, France
b Department of Membrane Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany
c European Synchrotron Radiation Facility, B.P. 220, 38043 Grenoble, France
d Dipartimento di Scienze Fisiche ed Astronomiche, Universita di Palermo, Via Archirafi 36, 90123, Palermo, Italy
e Forschungsneutronenquelle Heinz Maier-Leibnitz (FRM II), 85747 Garching, Germany
f Technische Universitaet Muenchen, Physik Department E21, Lichtenbergstrasse 1, 85747 Garching, Germany
g INFM-CNR OGG & CRS-SOFT, c/o ILL, 6 Rue Jules Horowitz, BP 156-38042, Grenoble Cedex 9, France
h Dipartimento di Fisica, Universita di Perugia, Via Pascoli, 06123 Perugia, Italy
i CNR-INFM CRS SOFT c/o Dipartimento di Fisica, Universita La Sapienza, p.le Aldo Moro 4, 00185 Roma, Italy
j European Laboratory for Non-Linear Spectroscopy, University of Florence, Via N. Carrara 1, 50019 Sesto Fiorentino, Italy (literal)
- Titolo
- A benchmark for protein dynamics: Ribonuclease A measured by neutron scattering in a large wavevector-energy transfer range (literal)
- Abstract
- The dynamics of Ribonuclease A was explored in the full range of time and length-scales accessible by neutron spectroscopy, on timeof-
flight, backscattering and spin-echo spectrometers. Samples were examined in dry and hydrated powder forms and in concentrated
and dilute solutions. The aim of the study was an experimental characterisation of the full variety of protein dynamics arising from stabilisation
forces. The results provide a benchmark against which other sample dynamics can be compared. (literal)
- Prodotto di
- Autore CNR
- Insieme di parole chiave
Incoming links:
- Autore CNR di
- Prodotto
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
- Insieme di parole chiave di