Báo cáo khoa học: The Alzheimer b-peptide shows temperature-dependent transitions between left-handed 31-helix, b-strand and random coil secondary structures
Số trang: 12
Loại file: pdf
Dung lượng: 363.35 KB
Lượt xem: 7
Lượt tải: 0
Xem trước 2 trang đầu tiên của tài liệu này:
Thông tin tài liệu:
The temperature-induced structural transitions of the full length Alzheimeramyloid b-peptide [Ab(1–40) peptide] and fragments of it were studiedusing CD and1H NMR spectroscopy. The full length peptide undergoesan overall transition from a state with a prominent population of left-handed 31 (polyproline II; PII)-helix at 0C to a random coil state at60C, with an averageDH of 6.8 ± 1.4 kJÆmol)1per residue, obtained byfitting a Zimm–Bragg model to the CD data.
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: The Alzheimer b-peptide shows temperature-dependent transitions between left-handed 31-helix, b-strand and random coil secondary structures
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: The Alzheimer b-peptide shows temperature-dependent transitions between left-handed 31-helix, b-strand and random coil secondary structures
Tìm kiếm theo từ khóa liên quan:
scientific reports Report medicine traditional medicine medicine cell proliferation oxidationGợi ý tài liệu liên quan:
-
9 trang 20 0 0
-
Ebook Cancer biology (3/E): Part 2
165 trang 19 0 0 -
Encyclopedia of Medical Anthropology
1119 trang 19 0 0 -
Báo cáo khoa học: Programmed cell death Apoptosis and alternative deathstyles
13 trang 19 0 0 -
63 trang 19 0 0
-
Oxford Living Grammar Intermediate 1
79 trang 17 0 0 -
11 trang 16 0 0
-
138 trang 15 0 0
-
12 trang 15 0 0
-
Báo cáo khoa học: Lpx1p is a peroxisomal lipase required for normal peroxisome morphology
11 trang 14 0 0