木桶(钟表)
电压依赖性阴离子通道
核磁共振波谱
化学
VDAC1型
C端
N端
结晶学
生物物理学
构象变化
固态核磁共振
脂质双层
立体化学
生物化学
肽序列
材料科学
氨基酸
物理
生物
膜
细菌外膜
核磁共振
大肠杆菌
基因
复合材料
作者
Robert C. Schneider,Manuel Etzkorn,Karin Giller,Venita Daebel,Jörg Eisfeld,Markus Zweckstetter,Christian Griesinger,Stefan Becker,Adam Lange
标识
DOI:10.1002/anie.200906241
摘要
Roll out the barrel: The conformation of the N-terminal domain of a functional human voltage-dependent anion channel (hVDAC1) in lipid bilayers has been determined (see picture; overlay of NMR model (blue) and X-ray structure (red/gray)). Solid-state NMR spectroscopy reveals that the N terminus assumes a well-defined, rigid structure and that its removal induces a conformational change in the hVDAC1 β-barrel.
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