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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment
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The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment

机译:用tri轰击评估甲型流感病毒基质蛋白M1的原位空间排列

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摘要

Intact influenza A virions were bombarded with thermally activated tritium atoms and the intramolecular distribution of the label in the matrix protein M1 was analyzed to determine the in situ accessibility of its tryptic fragments. These data were combined with the previously reported X-ray crystal structure of the M1 fragment 2-158 [Sha,B& luo, M.(1997) nat.Struct. Biol. 4,239-244] and the predicted topology of the C domain (159-252) to propose a model of M1 arrangement in the virus particle.
机译:用热活化的atoms原子轰击完整的甲型流感病毒粒子,并分析基质蛋白M1中标记物的分子内分布,以确定其胰蛋白酶消化片段的原位可及性。这些数据与先前报道的M1片段2-158的X射线晶体结构相结合[Sha,B&luo,M。(1997)nat.Struct。生物学[4239-244]和C结构域的预测拓扑(159-252)以提出病毒颗粒中M1排列的模型。

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