ガス相におけるペプチド二次構造:N結合グリコプロテインのコンセンサスモチーフ
Emilio J Cocinero1, E Cristina Stanca-Kaposta, David P Gamblin
1Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QZ, United Kingdom.
Journal of the American Chemical Society
|January 1, 2009
まとめ
二次構造は,N-リンクされたグリコプロテインのNXS/Tシーコンに影響を与える. ガス相スペクトロスコーピーと計算により,異なる形状が明らかになり,酵素性グリコシル化に関する洞察が得られます.
科学分野:
- バイオケミストリー バイオケミストリー
- 構造生物学 構造生物学とは
- コンピューティング・ケミストリー
背景:
- N-リンクされたグリコシレーションは,タンパク質の機能にとって極めて重要です.
- コンセンサスシーコンNXS/Tは,N-リンクされたグリコプロテイン全体で保存されます.
- 配列選択における本質的二次構造の役割は議論されている.
研究 の 目的:
- NXS/T配列をモデリングするペプチドの固有の二次構造を調査する.
- 二次構造がグリコシル化部位の選択にどのように影響するかを決定する.
- ペプチド構成と酵素によるグリコシル化との関係を調査する.
主な方法:
- ガス相における赤外線レーザーイオン浸透スペクトロスコーピー.
- アブ・イニシオと密度関数理論の計算.
- キャップされたオリゴペプチド (Ac-NGS-NHBn,Ac-QGS-NHBn,Ac-NPS-NHBn) の分析.
主要な成果:
- NGSは,溶液相アックスターンと異なるS形状の形状を採用しています.
- QGSは,より強い水素結合を持つより硬い構造を示しています.
- NPSは,結晶構造に似たC(10) ベータターンでAsxターンを形成します.
- 形状的差異は,サイドチェーン相互作用と潜在的反応性と相関する.
結論:
- 内在の二次構造は,コンセンサス順序を決定する上で重要な役割を果たします.
- ガス相構造は,環境要因により溶液と結晶構造と異なる.
- 構造的制約は,アスパラジンの酵素性グリコシル化についての洞察を提供します.
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