Dynamics of myoglobin in confinement: An elastic and quasi-elastic neutron scattering study (Articolo in rivista)

Type
Label
  • Dynamics of myoglobin in confinement: An elastic and quasi-elastic neutron scattering study (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Alternative label
  • Schiro, G; Sclafani, M; Caronna, C; Natali, F; Plazanet, M; Cupane, A (2008)
    Dynamics of myoglobin in confinement: An elastic and quasi-elastic neutron scattering study
    in Chemical physics (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Schiro, G; Sclafani, M; Caronna, C; Natali, F; Plazanet, M; Cupane, A (literal)
Pagina inizio
  • 259 (literal)
Pagina fine
  • 266 (literal)
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  • 345 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • \"[Schiro, Giorgio; Sclafani, Michele; Caronna, Chiara; Cupane, Antonio] Univ Palermo, CNISM, I-90123 Palermo, Italy; [Natali, Francesca] ILL, INFM CNR OGG & CRS SOFT, F-38042 Grenoble, France; [Plazanet, Marie] Inst Max Von Laue Paul Langevin, F-38042 Grenoble, France; [Schiro, Giorgio; Sclafani, Michele; Caronna, Chiara; Cupane, Antonio] Univ Palermo, Dept Phys & Astron Sci, I-90123 Palermo, Italy (literal)
Titolo
  • Dynamics of myoglobin in confinement: An elastic and quasi-elastic neutron scattering study (literal)
Abstract
  • In order to clarify the role of hard confinement on protein dynamics, elastic and quasi-elastic neutron scattering experiments have been performed on ferric horse myoglobin in two different systems: the protein embedded in a porous silica matrix, and the corresponding hydrated protein powder. Elastic data have been analysed using two different models (dynamical heterogeneity and anharmonic double-well potential) that take into account deviations of elastic intensity from Gaussian behaviour. The profile of quasi-elastic spectra has been approximated by a combination of Lorentzian and Gaussian components. Comparison between the data relative to the two different samples indicates that geometrical confinement within the matrix plays a crucial role in protein dynamics and conformational stability, the effect of sol-gel encapsulation being essentially a reduction of large scale protein motions (alpha-relaxation) likely related to the slowing down of solvent confined diffusion. (C) 2007 Elsevier B.V. All rights reserved. (literal)
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