双层
化学
膜
脂质双层融合
结晶学
脂质双层
模型脂质双层
氢键
胶束
生物物理学
质子化
侧链
极地的
离子
脂质双层相行为
生物化学
水溶液
分子
有机化学
生物
物理
天文
聚合物
作者
Steven R. Van Doren,Benjamin S. Scott,Rama K. Koppisetti
出处
期刊:Structure
[Elsevier]
日期:2023-10-01
卷期号:31 (10): 1184-1199.e3
标识
DOI:10.1016/j.str.2023.07.015
摘要
The fusion peptide of SARS-CoV-2 spike is essential for infection. How this charged and hydrophobic domain occupies and affects membranes needs clarification. Its depth in zwitterionic, bilayered micelles at pH 5 (resembling late endosomes) was measured by paramagnetic NMR relaxation enhancements used to bias molecular dynamics simulations. Asp830 inserted deeply, along with Lys825 or Lys835. Protonation of Asp830 appeared to enhance agreement of simulated and NMR-measured depths. While the fusion peptide occupied a leaflet of the DMPC bilayer, the opposite leaflet invaginated with influx of water and choline head groups in around Asp830 and bilayer-inserted polar side chains. NMR-detected hydrogen exchange found corroborating hydration of the backbone of Thr827-Phe833 inserted deeply in bicelles. Pinching of the membrane at the inserted charge and the intramembrane hydration of polar groups agree with theory. Formation of corridors of hydrated, inward-turned head groups was accompanied by flip-flop of head groups. Potential roles of the defects are discussed.
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