Conditioning action of the environment on the protein dynamics studied through elastic neutron scattering (Articolo in rivista)

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Label
  • Conditioning action of the environment on the protein dynamics studied through elastic neutron scattering (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s00249-006-0073-7 (literal)
Alternative label
  • A. Paciaroni (1); E. Cornicchi (1); A. De Francesco (2); M. Marconi (1); G. Onori (1) (2006)
    Conditioning action of the environment on the protein dynamics studied through elastic neutron scattering
    in European biophysics journal
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • A. Paciaroni (1); E. Cornicchi (1); A. De Francesco (2); M. Marconi (1); G. Onori (1) (literal)
Pagina inizio
  • 591 (literal)
Pagina fine
  • 599 (literal)
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  • 35 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 9 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • (1) Dipartimento di Fisica dell'Universit√† di Perugia, CNR-INFM CRS SOFT, Via A. Pascoli, 06123 Perugia, Italy c/o Dipartimento di Chimica dell'Universit√† di Perugia, CEMIN (Centro di Eccellenza per i Materiali Innovativi e Nanostrutturati), Via Elce di Sotto 8, 06123 Perugia, Italy (2) CNR-INFM CRS SOFT, 00185 Rome, Italy c/o Institut Laue-Langevin, Rue Jules Horowitz 6, 38042 Grenoble, France (literal)
Titolo
  • Conditioning action of the environment on the protein dynamics studied through elastic neutron scattering (literal)
Abstract
  • The dynamics of lysozyme in the picosecond timescale has been studied when it is in dry and hydrated powder form and when it is embedded in glycerol, glycerol-water, glucose and glucose-water matrices. The investigation has been undertaken through elastic neutron scattering technique on the backscattering spectrometer IN13. The dynamics of dry powder and embedded-in-glucose lysozyme can be considered purely vibrational up to 100 K, where the onset of an anharmonic contribution takes place. This contribution can be attributed to the activation of methyl group reorientations and is described with an Arrhenius trend. An additional source of anharmonic dynamics appears at higher temperatures for lysozyme in hydrated powders and embedded in glycerol, glycerol-water and glucose-water matrices. This second process, also represented with an Arrhenius trend, corresponds to the so-called protein dynamical transition. Both the temperature where such a transition takes place and the magnitude of the protein mean square displacements depend on the environment. The dynamical response of the protein to temperature is put in relationship with its thermal stability. (literal)
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