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Updated: Jul 19, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

サミア・シンティア・リシニのシルクタンパク質繊維の混合ベータシート構造の分析に関連して,反並列および並列ベータシート構造を持つアラニン三ペプチドの構造分析は,固体NMRスペクトロスコピーを用いた固体NMRスペクトロスコピーを用いた

Tetsuo Asakura1, Michi Okonogi, Yasumoto Nakazawa

  • 1Department of Biotechnology, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo 184-8588, Japan. asakura@cc.tuat.ac.jp

Journal of the American Chemical Society
|May 4, 2006
PubMed
まとめ

固体核磁共振 (NMR) は,タンパク質の繊維構造を区別する. パラレルベータシートにおけるより長いスピン・レッツ relaxation times (T1) は,反パラレル構造からの差異化に役立ちます.

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Protein Organization01:13

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A protein's shape is critical to its function. For example, an enzyme can...
Protein Organization01:24

Protein Organization

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Protein Folding01:25

Protein Folding

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Structure of Amines01:19

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The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’ carbon–carbon bond (154 pm). These aspects are illustrated in Figure...