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- W2019227477 abstract "We have studied by X-ray diffraction and infrared spectroscopy the structure of the following peptides: N-acetyl-Lys-Ala-Tyr-Ala-Lys-ethylamide; N-acetyl-Lys-d(Ala)-Tyr-Ala-Lys-ethylamide; N-acetyl-Lys-Ala-Lys-Ala-Lys-ethylamide; N-acetyl-Lys-Ala-Lys-ethylamide and N-acetyl-Tyr-Ala-Lys-ethyalmide. All of them show a cross-β structure, most likely with an antiparallel organization of the peptide chains. The d-Ala residue present in one of the peptides apparently does not interfere with the formation of the pleated-sheet structure. Due to the sequence of the peptides we have used, most of them are organized in double layers: one hydrophobic, containing the methyl groups of alanine, and the other one hydrophilic, containing the lysine side chains. Tyrosine is also found in the latter layer." @default.
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- W2019227477 date "2009-01-12" @default.
- W2019227477 modified "2023-10-12" @default.
- W2019227477 title "Conformation of some oligopeptides containing Lys, Ala, and Tyr" @default.
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- W2019227477 doi "https://doi.org/10.1111/j.1399-3011.1985.tb02159.x" @default.
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