Structural features and conformational equilibria of 3-10-helical peptides in solution by spectroscopic and molecular mechanics studies (Articolo in rivista)

Type
Label
  • Structural features and conformational equilibria of 3-10-helical peptides in solution by spectroscopic and molecular mechanics studies (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Alternative label
  • Pispisa B., Mazzuca C., Palleschi A., Stella L., Venanzi M., Formaggio F., Toniolo C., Broxterman Q.B. (2002)
    Structural features and conformational equilibria of 3-10-helical peptides in solution by spectroscopic and molecular mechanics studies
    in Biopolymers (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Pispisa B., Mazzuca C., Palleschi A., Stella L., Venanzi M., Formaggio F., Toniolo C., Broxterman Q.B. (literal)
Pagina inizio
  • 247 (literal)
Pagina fine
  • 250 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 67 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Structural features and conformational equilibria of 3-10-helical peptides in solution by spectroscopic and molecular mechanics studies (literal)
Abstract
  • The structural features and conformational equilibria of a series of short, linear C-alpha-methylvaline [(alphaMe)Val]-based peptides in methanol were investigated by combining fluorescence resonance energy transfer measurements and molecular mechanics data. IR spectra were employed to determine their secondary structure, which exhibits an intramolecularly H-bonded, 3-10-helix conformation that is affected by backbone distortions that are enhanced by the shortness of the main chain. (literal)
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