Control of peptide conformation by the Thorpe-Ingold effect (C-alpha-tetrasubstitution) (Articolo in rivista)

Type
Label
  • Control of peptide conformation by the Thorpe-Ingold effect (C-alpha-tetrasubstitution) (Articolo in rivista) (literal)
Anno
  • 2001-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1002/bip.10184 (literal)
Alternative label
  • Toniolo C., Crisma M., Formaggio F., Peggion C. (2001)
    Control of peptide conformation by the Thorpe-Ingold effect (C-alpha-tetrasubstitution)
    in Biopolymers (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Toniolo C., Crisma M., Formaggio F., Peggion C. (literal)
Pagina inizio
  • 396 (literal)
Pagina fine
  • 419 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • Citazioni WOS: 343 Impact Factor 2001: 1.845 Coautore (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 60 (literal)
Rivista
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  • Fascicolo uscito nel 2002 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biomolecular Chemistry, CNR, Department of Organic Chemistry, University of Padova, 35131 Padova, Italy (literal)
Titolo
  • Control of peptide conformation by the Thorpe-Ingold effect (C-alpha-tetrasubstitution) (literal)
Abstract
  • The preferred conformations of peptides heavily based on the currently extensively exploited achiral and chiral alpha-amino acids with a quaternary alpha-carbon atom, as determined by conformational energy computations, crystal-state (X-ray diffraction) analyses, and solution (NMR and spectroscopic) investigations, are reviewed. It is concluded that 3(10)/alpha-helical structures and the fully-extended (C-5) conformation are preferentially adopted by peptide sequences characterized by this family of amino acids, depending upon overall bulkiness and nature (e.g., whether acyclic or C-alpha - C-alpha cyclized) of their side chains. (literal)
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