The conformational preferences of the alicyclic Cαα-disubstituted glycines Acnc (1-amino-1-cycloalkane-carboxylic acid; n = 4,7, 9, 12) were assessed in selected model compounds, including homopeptides and Ala (orAib, α-aminoisobutyric acid )/Acnc peptides containing a small total number of residues, by Fourier transform ir absorption,1H-nmr, and x-ray diffraction analyses. The results obtained indicate that β-turn and 310-helical structures are preferentially adopted by short peptides rich in these cycloaliphatic α-amino acids. © 1997 John Wiley & Sons, Inc.
Preferred conformation of peptides rich in alicyclic C-alpha,C-alpha-disubstituted glycines
IACOVINO, Rosa;
1996
Abstract
The conformational preferences of the alicyclic Cαα-disubstituted glycines Acnc (1-amino-1-cycloalkane-carboxylic acid; n = 4,7, 9, 12) were assessed in selected model compounds, including homopeptides and Ala (orAib, α-aminoisobutyric acid )/Acnc peptides containing a small total number of residues, by Fourier transform ir absorption,1H-nmr, and x-ray diffraction analyses. The results obtained indicate that β-turn and 310-helical structures are preferentially adopted by short peptides rich in these cycloaliphatic α-amino acids. © 1997 John Wiley & Sons, Inc.File in questo prodotto:
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