Homochiral (alphaMe)Leu/Ala and Leu/Ala model peptides were synthesized by solution methods and fully characterized. A solution conformational analysis of the tripeptides was carried out using FT-IR absorption and H-1 NMR. The crystal-state structure of Z-D-(alphaMe)Leu-(D-Ala)2-OMe monohydrate was resolved by X-ray diffraction. The results obtained support the conclusion that the tendency of the non-coded (alphaMe)Leu residue to fold into beta-bends and helical structures is markedly higher than that of its unmethylated protein counterpart (Leu).
Peptides From Chiral C(alpha,alpha)-disubstituted Glycines - Synthesis and Conformational-analysis of Homochiral (alpha-me) Leu/ala Model Peptides
FORMAGGIO, FERNANDO;TONIOLO, CLAUDIO
1994
Abstract
Homochiral (alphaMe)Leu/Ala and Leu/Ala model peptides were synthesized by solution methods and fully characterized. A solution conformational analysis of the tripeptides was carried out using FT-IR absorption and H-1 NMR. The crystal-state structure of Z-D-(alphaMe)Leu-(D-Ala)2-OMe monohydrate was resolved by X-ray diffraction. The results obtained support the conclusion that the tendency of the non-coded (alphaMe)Leu residue to fold into beta-bends and helical structures is markedly higher than that of its unmethylated protein counterpart (Leu).File in questo prodotto:
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