Abstract
The structural preferences of homopeptides from Aib(α-aminoisobutyric acid), Deg(Cα , α-diethylglycine), Dpg(Cα , α-dipropylglycine) and Ac n c(1-aminocycloalkane-1-carboxylic acid; n=3,5,6) residues, as determined by conformational energy computations, X-ray diffraction analyses, and spectroscopic studies, are reviewed. The results obtained indicate that the 3 10 -helix and the fully extended (C 5 ) conformation are preferentially adopted by long sequences of these Cα , α-disubstituted α-amino acid residues, depending upon bulkiness and nature (whether linear or cyclic) of their side chains
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