http://www.cnr.it/ontology/cnr/individuo/prodotto/ID15511
Uncommon, but emerging, alpha-peptide conformations (Articolo in rivista)
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- 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.)
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- F. Formaggio, M. Crisma, C. Toniolo (literal)
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- Citazioni WOS: 0
Impact Factor 2007: 0.318
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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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