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- W4205087337 abstract "The HPLC retention behavior of three complete single methionine and methionine sulfoxide replacement sets of two 18-mer model peptides and neuropeptide Y (NPY) were investigated. All peptides were prepared by multiple solid-phase peptide synthesis. Plotting the retention time differences between methionine and methionine sulfoxide analogues vs the position of replacement shows that potentially α-helical peptides become helical on binding during reversed-phase high performance liquid chromatography. In the case of an amphipathic α-helix, the retention time differences change periodically with a 3–4 repeat pattern, which allow the location of amphipathic helical structures. Replacements in nonamphipathic α-helical domains cause local preferential binding areas and lead to sequence-dependent retention time profiles. Methionine replacement studies of NPY suggest an unstructured or extended conformation from Tyr1 to Ala12 connected to a well-defined amphipathic α-helix from Pro13 to Arg35. The assignment is confirmed by comparison of nuclear Overhauser effects based two-dimensional 1H-nmr spectroscopy and utilization of the CαH shift index method in 50% trifluoroethanol/50% water. © 1996 John Wiley & Sons, Inc." @default.
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- W4205087337 date "1996-08-01" @default.
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- W4205087337 title "Assignment of the helical structure in neuropeptide Y by HPLC studies of methionine replacement analogues and 1H‐NMR spectroscopy" @default.
- W4205087337 doi "https://doi.org/10.1002/(sici)1097-0282(199608)39:2<207::aid-bip9>3.3.co;2-m" @default.
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