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- W2042645191 abstract "The conformational structure of the tetrapeptide Boc–Aib–Leu–Leu–Aib–OMe has been investigated by the PCILO method. The computational results show the formation of two closed β-turns, both of which are of type III, and the peptide backbone folds into a right-handed 310-helical conformation stabilized by two intramolecular 4 → 1 hydrogen bonds. The helix thus formed generates a pore of ∼3 Å along helix axis with hydrophobic amino acid side chains located on the outside of the helix, and this tendency of leucine side chains may enable leucinostatin A to fit into the membrane bilayer. The pore thus formed is cation-selective, and through this pore, the cation can pass only in a single file." @default.
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- W2042645191 date "1992-06-20" @default.
- W2042645191 modified "2023-09-24" @default.
- W2042645191 title "Conformational structure of the tetrapeptide Boc-Aib-Leu-Leu-Aib-OMe-the central fragment of the nonapeptide antibiotic leucinostatin A" @default.
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- W2042645191 doi "https://doi.org/10.1002/qua.560420606" @default.
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