期刊
ORGANIC LETTERS
卷 11, 期 14, 页码 3092-3095出版社
AMER CHEMICAL SOC
DOI: 10.1021/ol901181b
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资金
- Australian Research Council
A protein alpha-helix is defined by 3.6 amino acids per turn. Cyclization of the tripeptide Alanine-Leucine-Glutamate through a side chain to the N-terminus lactam bond produces cyclo-(1,3)-[ALE]-NH2 which displays a circular dichroism spectrum typical of an alpha-helix backbone. However, proton NMR spectra show a novel cyclic peptide featuring two non-hydrogen-bonded antiparallel beta-strands connected by an Ala-Leu cis-amide bond. This example highlights that the common practice of characterizing alpha-helices by CD spectra alone can be misleading.
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