Looking for a robust, synthetic, fully-extended [2.0(5)-helical peptide structure - effect of terminal groups (Articolo in rivista)

Type
Label
  • Looking for a robust, synthetic, fully-extended [2.0(5)-helical peptide structure - effect of terminal groups (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/ejoc.201101273 (literal)
Alternative label
  • Formaggio F.; Crisma M. ; Peggion C. ; Moretto A. ; Venanzi M. ; Toniolo C. (2012)
    Looking for a robust, synthetic, fully-extended [2.0(5)-helical peptide structure - effect of terminal groups
    in European journal of organic chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Formaggio F.; Crisma M. ; Peggion C. ; Moretto A. ; Venanzi M. ; Toniolo C. (literal)
Pagina inizio
  • 167 (literal)
Pagina fine
  • 174 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1-4,6: ICB, Padova Unit, CNR, Department of Chemical Sciences, University of Padova, 35131 Padova, Italy; 5: Department of Chemical Sciences and Technologies, University of Rome \"Tor Vergata\", 00133 Rome, Italy (literal)
Titolo
  • Looking for a robust, synthetic, fully-extended [2.0(5)-helical peptide structure - effect of terminal groups (literal)
Abstract
  • The incorporation of alpha-amino acids with a quaternary alpha-carbon atom into a peptide provides a tool to effectively restrict the available range of its backbone conformations. Specifically, under favorable conditions, C-alpha,alpha-diethylglycine (Deg) homopeptides are known to preferentially adopt the fully-extended [2.0(5)-helical] structure, which is characterized by the longest possible separation between two adjacent alpha- amino acid C-alpha atoms. We have investigated the influence of the nature of the N- and/or C-terminal protecting (or blocking) groups on the relative stabilities of the fully-extended conformation vs. the competing, shorter 3(10)-helical structure in a synthetic Deg homopeptide series. (literal)
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