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- W1974770897 abstract "Abstract The 13 C-NMR spectra of the synthetic membrane modifying nonadecapeptide Boc-(Aib- l -Ala) 5 -Gly-Ala-Aib-Pro-Ala- Aib-Aib-Glu(OBz)-Gln-OMe (Aib = α-aminoisobutyric acid), and of synthetic intermediates were used for conformational analysis in solution. The assignments of the 13 C-NMR signals of Aib are based on the magnetic nonequivalence (MNE) of the geminal C β -signals in asymmetric environment resulting in a shift difference of 0.2–0.5 ppm due to neighbouring chiral residues. More than 4 ppm MNE are observed due to α-helical conformation and about 2.5 ppm for Aib situated in the corners of a rigid β-turn. The Ala-C α signal is also sensitive to different secondary structures. The C α signal for C-terminal alanine is found at 49–50 ppm, and for alanine within unordered oligopeptides it absorbs at 50–51 ppm. α-Helical environment shifts the Ala-C α signal to lower field down to 54 ppm. In methanolic solution the nonadecapeptide shows a α-helical N-terminal region. For the C-terminus beginning with proline-14 no periodically ordered conformation is observed, and we suggest a sequence of β-turns. Furthermore the typical E/Z isomerism of the prolyl-peptide bond can be observed on proline itself and on its neighbour alanine." @default.
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- W1974770897 date "1982-01-01" @default.
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- W1974770897 title "13C-NMR und konformation eines membran-modifizierenden synthetischen nonadekapeptid-analogons von alamethicin und seiner zwischenstufen" @default.
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- W1974770897 doi "https://doi.org/10.1016/0040-4020(82)85163-6" @default.
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