http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14748
New tools for the control of peptide conformation and supramolecular chemistry: crown-carrier, C-alpha-methyl L-DOPA amino acids (Articolo in rivista)
- Type
- Label
- New tools for the control of peptide conformation and supramolecular chemistry: crown-carrier, C-alpha-methyl L-DOPA amino acids (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/bip.10594 (literal)
- Alternative label
Formaggio F., Oancea S., Peggion C., Crisma M., Toniolo C., Wright K., Wakselman M., Mazaleyrat J.P. (2003)
New tools for the control of peptide conformation and supramolecular chemistry: crown-carrier, C-alpha-methyl L-DOPA amino acids
in Biopolymers (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Formaggio F., Oancea S., Peggion C., Crisma M., Toniolo C., Wright K., Wakselman M., Mazaleyrat J.P. (literal)
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
- Citazioni WOS: 8
Impact Factor 2003: 2.733
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
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- 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;
SIRCOB, UMR CNRS 8086, Bat. Lavoisier, University of Versailles, 78000 Versailles, France (literal)
- Titolo
- New tools for the control of peptide conformation and supramolecular chemistry: crown-carrier, C-alpha-methyl L-DOPA amino acids (literal)
- Abstract
- The preferred conformation of five, terminally protected, model peptide series to the hexamer level, based on three novel crowned, C-alpha-methyl L-DOPA amino acids combined with either L-Ala/Aib or Gly/Aib, were assessed in structure supporting solvents using FT-IR absorption, H-1 NMR, and CD techniques. The FT-IR absorption spectra strongly suggest that the contribution of the crowned C-alpha-tetrasubstituted residue to intramolecular H-banding is equivalent to that of Aib and is much more significant than that of either L-Ala or Gly. In addition, the H-1 NMR titrations and the CD patterns resemble those typically exhibited by (right-handed) 3(10)-helical structures. (literal)
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