Mechanical properties of single motor molecules studied by three-dimensional thermal force probing in optical tweezers
Mechanical properties of single motor molecules studied by three-dimensional thermal force probing in optical tweezers
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DOI：
10.1002/cphc.200301027
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发表时间：
2004-08-20
期刊：
影响因子：
2.9
通讯作者：
Florin, EL
中科院分区：
文献类型：
--
作者：
Jeney, S;Stelzer, EHK;Florin, EL
将光阱中三维力的测量与热致（布朗）位置涨落的分析相结合，研究了分子马达驱动蛋白的力学性质.一个驱动蛋白分子连接到探针结合在一个严格的状态微管。光阱保持较弱以测量作用在探针上的热力，该热力主要由驱动蛋白系链抵消。测量了驱动蛋白在拉伸和压缩过程中相对于其主链轴的刚度。我们的研究结果表明，一节驱动蛋白接近电机域是占主导地位的元件在电机结构的灵活性。实验证明了3D热波动分析的功率来表征单个马达蛋白质的机械特性，并表明其在一般情况下研究单分子的有用性。
A new method combining three-dimensional (3D) force measurements in an optical trap with the analysis of thermally induced (Brownian) position fluctuations of a trapped probe was used to investigate the mechanical properties of a single molecule, the molecular motor kinesin. One kinesin molecule attached to the probe was bound in a rigorlike state to one microtubule. The optical trap was kept weak to measure the thermal forces acting on the probe, which were mainly counterbalanced by the kinesin tether. The stiffness of kinesin during stretching and compression with respect to its backbone axis were measured. Our results indicate that a section of kinesin close to the motor domain is the dominating element in the flexibility of the motor structure. The experiments demonstrate the power of 3D thermal fluctuation analysis to characterize mechanical properties of individual motor proteins and indicate its usefulness to study single molecule in general.