Physical Origin of Anharmonic Dynamics in Proteins: New Insights From Resolution-Dependent Neutron Scattering on Homomeric Polypeptides (Articolo in rivista)

Type

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

Label

• Physical Origin of Anharmonic Dynamics in Proteins: New Insights From Resolution-Dependent Neutron Scattering on Homomeric Polypeptides (Articolo in rivista) (literal)

Anno

• 2012-01-01T00:00:00+01:00 (literal)

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

• 10.1103/PhysRevLett.109.128102 (literal)

Alternative label

• Schiro, Giorgio; Natali, Francesca; Cupane, Antonio (2012)
  Physical Origin of Anharmonic Dynamics in Proteins: New Insights From Resolution-Dependent Neutron Scattering on Homomeric Polypeptides
  in Physical review letters (Print)
  (literal)

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

• Schiro, Giorgio; Natali, Francesca; Cupane, Antonio (literal)

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

• 109 (literal)

Rivista

• Physical review letters (Rivista)

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

• 5 (literal)

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

• 12 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• University of Palermo - Italy; Institute Laue Langevin (literal)

Titolo

• Physical Origin of Anharmonic Dynamics in Proteins: New Insights From Resolution-Dependent Neutron Scattering on Homomeric Polypeptides (literal)

Abstract

• Neutron scattering reveals a complex dynamics in polypeptide chains, with two main onsets of anharmonicity whose physical origin and biological role are still debated. In this study the dynamics of strategically selected homomeric polypeptides is investigated with elastic neutron scattering using different energy resolutions and compared with that of a real protein. Our data spotlight the dependence of anharmonic transition temperatures and fluctuation amplitudes on energy resolution, which we quantitatively explain in terms of a two-site model for the protein-hydration water energy landscape. Experimental data strongly suggest that the protein dynamical transition is not a mere resolution effect but is due to a real physical effect. Activation barriers and free energy values obtained for the protein dynamical transition allow us to make a connection with the two-well interaction potential of supercooled-confined water proposed to explain a low-density -> high-density liquid-liquid transition. (literal)

Prodotto di

• MD.P02.016.001 Materia soffice: diffusione elastica ed anelastica di neutroni e raggi-x (MD.P02.016.002) (Modulo)

Autore CNR

• FRANCESCA NATALI (Persona)

Incoming links:

Autore CNR di

• FRANCESCA NATALI (Persona)

Prodotto

• MD.P02.016.001 Materia soffice: diffusione elastica ed anelastica di neutroni e raggi-x (MD.P02.016.002) (Modulo)

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

• Physical review letters (Rivista)