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Báo cáo khoa học: The Alzheimer b-peptide shows temperature-dependent transitions between left-handed 31-helix, b-strand and random coil secondary structures

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

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The temperature-induced structural transitions of the full length Alzheimer amyloid b-peptide [Ab(1–40) peptide] and fragments of it were studied using CD and 1 H NMR spectroscopy. The full length peptide undergoes an overall transition from a state with a prominent population of left-handed 31 (polyproline II; PII)-helix at 0C to a random coil state at 60C, with an averageDH of 6.8 ± 1.4 kJÆmol )1 per residue, obtained by fitting a Zimm–Bragg model to the CD data.

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Nội dung Text: Báo cáo khoa học: The Alzheimer b-peptide shows temperature-dependent transitions between left-handed 31-helix, b-strand and random coil secondary structures

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