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Báo cáo khoa học: Elements of the C-terminal t peptide of acetylcholinesterase that determine amphiphilicity, homomeric and heteromeric associations, secretion and degradation

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:12

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The C-terminal t peptide (40 residues) of vertebrate acetyl-cholinesterase (AChE) T subunits possesses a series of seven conserved aromatic residues and forms an amphiphilic a-helix; it allows the formation of homo-oligomers (mono-mers, dimers and tetramers) and heteromeric associations with the anchoringproteins, ColQ and PRiMA, which contain a proline-rich motif (PRAD). We analyzed the influenceofmutations in the t peptideofTorpedoAChETon oligomerization and secretion.

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Nội dung Text: Báo cáo khoa học: Elements of the C-terminal t peptide of acetylcholinesterase that determine amphiphilicity, homomeric and heteromeric associations, secretion and degradation

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