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首页> 外文期刊>The FEBS journal >Proton-decoupled N-15 and P-31 solid-state NMR investigations of the Pf3 coat protein in oriented phospholipid bilayers
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Proton-decoupled N-15 and P-31 solid-state NMR investigations of the Pf3 coat protein in oriented phospholipid bilayers

机译:定向磷脂双层中Pf3外壳蛋白的质子解耦N-15和P-31固态NMR研究

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摘要

The coat proteins of filamentous phage are first synthesized as transmembrane proteins and then assembled onto the extruding viral particles. We investigated the transmembrane conformation of the Pseudomonas aeruginosa Pf3 phage coat protein using proton-decoupled N-15 and P-31 solid-state NMR spectroscopy. The protein was either biochemically purified and uniformly labelled with N-15 or synthesized chemically and labelled at specific sites. The proteins were then reconstituted into oriented phospholipid bilayers and the resulting samples analysed. The data suggest a model in which the protein adopts a tilted helix with an angle of approximate to 30 degrees and an N-terminal 'swinging arm' at the membrane surface.
机译:丝状噬菌体的外壳蛋白首先合成为跨膜蛋白,然后组装到挤出的病毒颗粒上。我们使用质子去耦的N-15和P-31固态NMR光谱研究了铜绿假单胞菌Pf3噬菌体外壳蛋白的跨膜构象。蛋白质经过生物化学纯化并用N-15均匀标记,或化学合成并在特定位点标记。然后将蛋白质重构为定向的磷脂双层,并分析所得的样品。数据提示了一种模型,其中蛋白质采用倾斜的螺旋结构,其角度约为30度,并在膜表面形成N端“摆动臂”。

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