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Báo cáo khoa học: Total chemical synthesis and NMR characterization of the glycopeptide tx5a, a heavily post-translationally modified conotoxin, reveals that the glycan structure is a-D-Gal-(1fi3)-a-D-GalNAc

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:11

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The 13-amino acid glycopeptide tx5a (Gla-Cys-Cys-Gla-Asp-Gly-Trp*-Cys-Cys-Thr*-Ala-Ala-Hyp-OH, where Trp*¼6-bromotryptophan and Thr*¼Gal-GalNAc-threonine), isolated fromConus textile, causes hyperactivity and spasticity when injected intracerebral ventricularly into mice. It contains nine post-translationallymodified residues: four cysteine residues, twoc-carboxyglutamic acid residues, and one residue each of 6-bromotryptophan, 4-trans-hydroxyproline and glycosylated threonine.

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Nội dung Text: Báo cáo khoa học: Total chemical synthesis and NMR characterization of the glycopeptide tx5a, a heavily post-translationally modified conotoxin, reveals that the glycan structure is a-D-Gal-(1fi3)-a-D-GalNAc

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