Comparative study of protein dynamics in hydrated powders and in solutions: A neutron scattering investigation (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Comparative study of protein dynamics in hydrated powders and in solutions: A neutron scattering investigation (Articolo in rivista) (literal)

Anno

• 2008-01-01T00:00:00+01:00 (literal)

Alternative label

• Marconi, M; Cornicchi, E; Onori, G; Paciaroni, A (2008)
  Comparative study of protein dynamics in hydrated powders and in solutions: A neutron scattering investigation
  in Chemical physics (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Marconi, M; Cornicchi, E; Onori, G; Paciaroni, A (literal)

Pagina inizio

• 224 (literal)

Pagina fine

• 229 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 345 (literal)

Rivista

• Chemical physics (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• \"[Paciaroni, A.] Univ Perugia, Dipartimento Fis, INFM CRS SOFT, Unita Perugia, I-06123 Perugia, Italy; Univ Perugia, Dipartimento Chim, CEMIN, I-06123 Perugia, Italy (literal)

Titolo

• Comparative study of protein dynamics in hydrated powders and in solutions: A neutron scattering investigation (literal)

Abstract

• Neutron scattering spectroscopy on a time-of-flight spectrometer has been exploited to reveal the vibrational and relaxational spectral contributions of lysozyme in hydrated powder and solution states. The inelastic component of the dynamical structure factor seems to be quite similar for lysozyme in both the solid- and the liquid-state samples, particularly for energies higher than similar to 4 meV. After the subtraction of this component, the quasielastic contribution is evaluated. In the case of hydrated lysozyme powder the quasielastic scattering follows a two-power law with a ballistic Gaussian decrease above similar to 2 meV. The quasielastic scattering of lysozyme in solution exhibits a rather similar trend but a much larger intensity. This may be related to the increase of both the number and the amplitudes of the confined diffusive processes related to protein side-chains motions at the protein surface. (C) 2007 Elsevier B.V. All rights reserved. (literal)

Autore CNR

• ALESSANDRO PACIARONI (Persona)
• GIUSEPPE ONORI (Persona)

Insieme di parole chiave

• Keywords of "Comparative study of protein dynamics in hydrated powders and in solutions: A neutron scattering investigation" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• ALESSANDRO PACIARONI (Persona)
• GIUSEPPE ONORI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Chemical physics (Rivista)

Insieme di parole chiave di

• Keywords of "Comparative study of protein dynamics in hydrated powders and in solutions: A neutron scattering investigation" (Insieme di parole chiave)