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SH1与肌球蛋白亚片段-1表面肌动蛋白结合位点之间的空间关系。

Spatial relationship between SH1 and the actin binding site on myosin subfragment-1 surface.

作者信息

Yamamoto K, Sekine T, Sutoh K

出版信息

FEBS Lett. 1984 Oct 15;176(1):75-8. doi: 10.1016/0014-5793(84)80914-x.

Abstract

To examine the spatial relationship between SH1 thiol and actin binding site on subfragment-1 surface, we studied the interaction with actin of subfragment-1 whose SH1 was labeled with an iodoacetate derivative of biotin and covered with avidin. Subfragment-1--avidin complex bound F-actin and its Mg2+ ATPase activity was activated by actin. Considering the size and the location of biotin binding site on avidin, our results suggest that SH1 is separated from the actin binding site on subfragment-1 surface by at least 17-20 A.

摘要

为了研究SH1巯基与肌动蛋白结合位点在亚片段-1表面的空间关系,我们研究了用生物素碘乙酸衍生物标记并被抗生物素蛋白覆盖的亚片段-1与肌动蛋白的相互作用。亚片段-1-抗生物素蛋白复合物结合F-肌动蛋白,其Mg2+ATP酶活性被肌动蛋白激活。考虑到抗生物素蛋白上生物素结合位点的大小和位置,我们的结果表明,SH1与亚片段-1表面的肌动蛋白结合位点至少相隔17-20埃。

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