Understanding Electron Transfer across Negatively-Charged Aib Oligopeptides. (Articolo in rivista)

Type
Label
  • Understanding Electron Transfer across Negatively-Charged Aib Oligopeptides. (Articolo in rivista) (literal)
Anno
  • 2005-01-01T00:00:00+01:00 (literal)
Alternative label
  • Improta, Roberto; Antonello, Sabrina; Formaggio, Fernando; Maran, Flavio; Rega, Nadia; Barone, Vincenzo. (2005)
    Understanding Electron Transfer across Negatively-Charged Aib Oligopeptides.
    in The journal of physical chemistry. B
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Improta, Roberto; Antonello, Sabrina; Formaggio, Fernando; Maran, Flavio; Rega, Nadia; Barone, Vincenzo. (literal)
Pagina inizio
  • 1023 (literal)
Pagina fine
  • 1033 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 109 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • Lavoro su rivista scientifica internazionale (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • The physicochemical effects modulating the conformational behavior and the rate of intramolecular dissociative electron transfer in phthalimide-Aib(n)-peroxide peptides (n = 0-3) have been studied by an integrated density functional/continuum solvent model. We found that three different orientations of the phthalimide fine are possible, labeled Phi(hel), Phi(C7), and Phi(pII). In the condensed phase. they are very close in energy when the system is neutral and short. When the peptide chain length increases and the system is negatively charged, Phi(hel) becomes instead the most stable conformer. Our calculations confirm that the 3(10)-helix is the most stable secondary structure for the peptide bridge. However, upon charge injection in the phthalimide end of the phthalimide-Aib(3)-peroxide, the peptide bridge can adopt an a-helix conformation as well. The study of the dependence of the frontier orbitals on the length and on the conformation of the peptide bridge (in agreement with experimental indications) suggests that for n = 3 the process could be influenced by a 3(10) --> alpha-helix conformational transition of the peptide chain (literal)
Titolo
  • Understanding Electron Transfer across Negatively-Charged Aib Oligopeptides. (literal)
Abstract
  • The physicochem. effects modulating the conformational behavior and the rate of intramol. dissociative electron transfer in peroxide peptides Pht-C(Me)2CO-[NHC(Me)2CO]n-O-O-CMe3 (I; n = 0-3; Pht = phthalimido) have been studied by an integrated d. functional/continuum solvent model. The authors found that three different orientations of the phthalimide ring are possible, labeled (phi)hel, (Phi)C7, and (Phi)pII. In the condensed phase, they are very close in energy when the system is neutral and short. When the peptide chain length increases and the system is neg. charged, (phi)hel becomes instead the most stable conformer. The calcns. confirm that the 310-helix is the most stable secondary structure for the peptide bridge. However, upon charge injection in the phthalimide end of I (n = 3), the peptide bridge can adopt an a-helix conformation as well. The study of the dependence of the frontier orbitals on the length and on the conformation of the peptide bridge (in agreement with exptl. indications) suggests that for I (n = 3) the process could be influenced by a 310/a-helix conformational transition of the peptide chain. (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it