Allosteric control through mechanical tension
Allosteric control through mechanical tension
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DOI：
10.1103/physrevlett.95.078102
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发表时间：
2005-08-12
影响因子：
8.6
通讯作者：
Perry, LJ
中科院分区：
文献类型：
--
作者：
Choi, B;Zocchi, G;Perry, LJ
蛋白质的构象变化调节其功能。在变构控制中，构象变化由信号分子的结合诱导。在这里，我们插入一个“分子弹簧”的酶鸟苷酸激酶，以控制这种蛋白质的构象。弹簧的刚度可以在外部变化，这允许人们在蛋白质表面上的弹簧附着的两点之间施加受控的机械张力。我们证明，通过施加和释放张力，我们可以可逆地关闭和打开酶。
Conformational changes of proteins modulate their function. In allosteric control, the conformational change is induced by the binding of a signaling molecule. Here we insert a "molecular spring" on the enzyme guanylate kinase, to control the conformation of this protein. The stiffness of the spring can be varied externally, which allows one to exert a controlled mechanical tension between the two points on the protein's surface where the spring is attached. We show that by applying and releasing the tension we can reversibly turn the enzyme off and on.