逆平行βシート
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- 1. アミロイド疾患の遺伝的要因genetic factors in the amyloid diseases [show details]
…precursors, which undergo conformational changes that lead to the adoption of a predominantly antiparallel beta-pleated sheet configuration . Amyloid deposits appear as amorphous hyaline material on light microscopy …
- 2. 食物アレルゲンの分子機能molecular features of food allergens [show details]
…that feed on stored cereal grains. AATIs consist of four to five alpha-helices and a short antiparallel beta sheet tightly held together by four to five intrachain disulfide bridges. AATIs have the capacity …
- 3. 免疫グロブリン軽鎖(AL)アミロイドーシスおよび軽鎖重鎖沈着症の病因pathogenesis of immunoglobulin light chain al amyloidosis and light and heavy chain deposition diseases [show details]
…deposition of insoluble fibrils as a result of protein misfolding. These fibrils have an antiparallel beta-pleated sheet configuration (noted on X-ray diffraction), and can be identified on biopsy specimens …
- 4. アミロイドーシスの概要overview of amyloidosis [show details]
…which have undergone conformational changes that lead to the adoption of a predominantly antiparallel beta-pleated sheet configuration. Multiple different human protein precursors of amyloid fibrils are known …
- 5. AAアミロイドーシスの発症機序pathogenesis of aa amyloidosis [show details]
…with regard to their primary structure or metabolism. The fibrils have a predominantly antiparallel beta-pleated sheet configuration; they can be identified on biopsy specimens by tinctorial properties that …
Japanese Journal
- Crystal Structure of Gramicidin S Hydrochloride at 1.1 Å Resolution
- ASANO Akiko,DOI Mitsunobu
- X-ray Structure Analysis Online 35(0), 1-2, 2019
- … Two independent peptide molecules were found, which formed antiparallel-sheets having intramolecular hydrogen bonds between Val and Leu residues. … The peptides turned at the <span style="font-variant: small-caps;">d</span>-Phe–Pro moieties, and the conformations were defined as type II' β-turn. … Adjacent molecules formed an angle of 49° and were arranged side-by-side to form a β-sheet along the <i>c</i>-axis.</p> …
- NAID 130007555332
- Purification, Cloning, Functional Expression, Structure, and Characterization of a Thermostable β-Mannanase from <i>Talaromyces trachyspermus </i>B168 and Its Efficiency in Production of Mannooligosaccharides from Coffee Wastes
- Suzuki Kentaro,Michikawa Mari,Sato Haruna,Yuki Masahiro,Kamino Kei,Ogasawara Wataru,Fushinobu Shinya,Kaneko Satoshi
- Journal of Applied Glycoscience 65(2), 13-21, 2018
- … <p>Highly thermostable β-mannanase, belonging to glycoside hydrolase family 5 subfamily 7, was purified from the culture supernatant of <i>Talaromyces trachyspermus </i>B168 and the cDNA of its transcript was cloned. … An antiparallel β-sheet, salt-bridges, hydrophobic packing, proline residues in the loops, and loop shortening are considered to be related to the thermostability of the enzyme. …
- NAID 130006742991
- グリシン,ジグリシン,トリグリシンを含む脂肪酸誘導体によるポリグリシンII構造の形成
- 野田 卓夢,近藤 沙南,荷堂 清香 [他],長谷川 健,山田 哲弘
- 高分子論文集 73(1), 69-75, 2016
- グリシン,ジグリシン,トリグリシンを部分構造とする脂肪酸型両親媒性分子を合成し,固体試料のFT-IRスペクトルを測定した.これらの化合物は,いずれもアミドI吸収帯が1650 cm<sup>-1</sup>と1640 cm<sup>-1</sup>に分裂する典型的なポリグリシンII構造(3<sub>1</s …
- NAID 130005120381
Related Links
- Amyloid fibril with parallel β-sheet configuration is formed at elevated temperature, while oligomer with antiparallel β-sheet configuration is formed at room temperature. The interplay between fibrillation and oligomerization suggests ...
- Purification of Antiparallel β-sheet Fibrils by Seeding and Filtration. Peptide synthesis and fibril formation are described in Supporting Information.Fig. 1A shows a transmission electron microscope (TEM) image of fibrils formed from initially monomeric D23N-Aβ 1–40 at 6 C in incubation buffer (10 mM sodium phosphate, pH 7.4, 0.01% NaN 3).
- Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils. Qiang W(1), Yau WM, Luo Y, Mattson MP, Tycko R. Author information: (1)Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney
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- antiparallel β-Sheet
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