Out-of-equilibrium versus dynamical and thermodynamical transitions (Articolo in rivista)

Type
Label
  • Out-of-equilibrium versus dynamical and thermodynamical transitions (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1143/PTPS.184.339 (literal)
Alternative label
  • Alberto Imparato (1); Stefano Luccioli (2,3); Alessandro Torcini (2,3) (2010)
    Out-of-equilibrium versus dynamical and thermodynamical transitions
    in Progress of theoretical physics. Supplement
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Alberto Imparato (1); Stefano Luccioli (2,3); Alessandro Torcini (2,3) (literal)
Pagina inizio
  • 339 (literal)
Pagina fine
  • 350 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Proceedings of the \"YKIS 2009 : Frontiers in Nonequilibrium Physics\" conference in Kyoto, August 2009. (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://ptp.ipap.jp/link?PTPS/184/339/ (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 184 (literal)
Rivista
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  • Proceedings of the \"YKIS 2009 : Frontiers in Nonequilibrium Physics\" conference in Kyoto, August 2009. Publication Office of Progress of Theoretical Physics. (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • (1) Dept. of Physics and Astronomy, University of Aarhus, Ny Munkegade, Building 1520 - DK-8000 Aarhus C, Denmark (2) Istituto dei Sistemi Complessi, CNR, via Madonna del Piano 10, I-50019 Sesto Fiorentino, Italy (3) INFN, Sez. Firenze, and CSDC, via Sansone, 1 - I-50019 Sesto Fiorentino, Italy (literal)
Titolo
  • Out-of-equilibrium versus dynamical and thermodynamical transitions (literal)
Abstract
  • Equilibrium and out-of-equilibrium transitions of an off-lattice protein model have been identified and studied. In particular, the out-of-equilibrium dynamics of the protein undergoing mechanical unfolding is investigated, and by using a work fluctuation relation, the system free energy landscape is evaluated. Three different structural transitions are identified along the unfolding pathways. Furthermore, the reconstruction of the the free and potential energy profiles in terms of inherent structure formalism allows us to put in direct correspondence these transitions with the equilibrium thermal transitions relevant for protein folding/unfolding. Through the study of the fluctuations of the protein structure at different temperatures, we identify the dynamical transitions, related to configurational rearrangements of the protein, which are precursors of the thermal transitions. (literal)
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