In situ molecular dynamics analysis of the water hydrogen bond at biomolecular sites: hydrophobicity enhances dynamics heterogeneity (Articolo in rivista)

Type

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

Label

• In situ molecular dynamics analysis of the water hydrogen bond at biomolecular sites: hydrophobicity enhances dynamics heterogeneity (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

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

• 10.1016/j.cplett.2011.10.031 (literal)

Alternative label

• Daniela Russo a,*, Eric Pellegrini b, Miguel Angel Gonzalez b, Stefania Perticaroli c, José Teixeira d (2011)
  In situ molecular dynamics analysis of the water hydrogen bond at biomolecular sites: hydrophobicity enhances dynamics heterogeneity
  in The journal of physical chemistry letters
  (literal)

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

• Daniela Russo a,*, Eric Pellegrini b, Miguel Angel Gonzalez b, Stefania Perticaroli c, José Teixeira d (literal)

Pagina inizio

• 80 (literal)

Pagina fine

• 85 (literal)

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

• 510 (literal)

Rivista

• ?The ?journal of physical chemistry letters (Rivista)

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

• a CNR-IOM c/o Institut Laue Langevin, 6 rue J. Horowitz BP156, F-38042 Grenoble, France b Institut Laue Langevin, 6 rue J. Horowitz BP156, F-38042 Grenoble, France c Università degli Studi di Perugia, Dipartimento di Chimica, Sezione di Chimica Fisica, via Elce di sotto 8, I-06123 Perugia, Italy d Laboratoire Léon Brillouin (CEA/CNRS), CEA Saclay, 91191 Gif-sur Yvette, Cedex, France (literal)

Titolo

• In situ molecular dynamics analysis of the water hydrogen bond at biomolecular sites: hydrophobicity enhances dynamics heterogeneity (literal)

Abstract

• Molecular dynamics simulations have been used to investigate the dynamics of hydrogen bonds (HBs) formed by hydration water in selected hydrophilic and hydrophobic biomolecules. Labelling all of atoms in the molecule allows analysing the HB relaxation time at specific donor and acceptor binding sites. The results show that the water-water HBs present a longer relaxation time around the completely hydro-philic peptide, and that the water-biomolecule HBs exhibit a distinct behaviour depending on the bind-ing sites at the hydrophilic or hydrophobic bio-interface. The presence of a large hydrophobic surface enhances, in particular at low temperature, the dynamical heterogeneity in the neighbouring hydrogen bond network. (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

• DANIELA RUSSO (Unità di personale interno)

Incoming links:

Autore CNR di

• DANIELA RUSSO (Unità di personale interno)

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

• ?The ?journal of physical chemistry letters (Rivista)