Uncommon, but emerging, alpha-peptide conformations (Articolo in rivista)

Type
Label
  • Uncommon, but emerging, alpha-peptide conformations (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Alternative label
  • F. Formaggio, M. Crisma, C. Toniolo (2007)
    Uncommon, but emerging, alpha-peptide conformations
    in Chimica oggi (Testo stamp.)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • F. Formaggio, M. Crisma, C. Toniolo (literal)
Pagina inizio
  • 28 (literal)
Pagina fine
  • 30 (literal)
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  • Citazioni WOS: 0 Impact Factor 2007: 0.318 Coautore (literal)
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  • 25 (literal)
Rivista
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  • 3 (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • Institute of Biomolecular Chemistry, Padova Unit, CNR, Department of Chemistry, University of Padova, 35131 Padova, Italy (literal)
Titolo
  • Uncommon, but emerging, alpha-peptide conformations (literal)
Abstract
  • Compared with the classical secondary structural elements of proteins [alpha-helix, beta-pleated sheets, isolated beta-turns, and Poly(Pro)(n) helix] other types of helical conformations [3(10)-helix and beta-turn ribbon spiral, gamma-helix, and 2.0(5)-helix] of peptides based on alpha-amino acids are currently emerging particularly from detailed analyses of appropriately designed model compounds. Their 3D-structural characterizations offer fascinating issues of precise control of probe-probe distances and relative orientations. Therefore, they present real potential to play a significant role as rigid, but easily tunable, spacers and templates in various areas of organic chemistry, supramolecular chemistry, and physical chemistry. (literal)
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