ISSN:
0006-3525
Keywords:
conformational analysis, of peptides
;
disubstituted glycines, peptides rich in
;
Fourier transform ir absorption, of peptides
;
310-helical conformation, in peptides
;
Cα-methylated α-amino acids, peptides rich in
;
nmr, of peptides
;
peptide conformation
;
x-ray diffraction, of peptides
;
β-turn conformation, in peptides
;
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The conformational preferences of the alicyclic Cα,α-disubstituted glycines Acnc (1-amino-1-cycloalkane-carboxylic acid; n = 4, 7, 9, 12) were assessed in selected model compounds, including homopeptides and Ala (or Aib, 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. Biopoly 40: 519-522, 1996
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
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