Mechanical Characterization of Motor Proteins: A Molecular Dynamics Approach

Aprodu I; Soncini M; Redaelli A

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Mechanical Characterization of Motor Proteins: A Molecular Dynamics Approach

机译：运动蛋白的机械表征：分子动力学方法

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A new approach, based on molecular dynamics, is presented to measure the mechanical properties of motor proteins, which are important for accomplishing their intracellular functions. Two different set-ups were designed to mimic the optical tweezers and surface force apparatus experiments. The results obtained show that the stiffness and elastic modulus of kinesin motor domain are 377 pN . nm(-1) and 0.17 GPa, respectively, while the myosin motor domain is characterized by a stiffness of 271 pN . nm(-1) and an elastic modulus of 0.26 GPa. These results suggest that the source of the very low stiffness detected for full-length molecules is located outside of the globular part of the proteins.

机译：提出了一种基于分子动力学的新方法来测量运动蛋白的机械性能，这对于完成其细胞内功能至关重要。设计了两种不同的设置来模拟光镊和表面力设备实验。结果表明，驱动蛋白运动域的刚度和弹性模量为377 pN。 nm（-1）和0.17 GPa，而肌球蛋白运动域的特征是271 pN的刚度。 nm（-1）和0.26 GPa的弹性模量。这些结果表明，为全长分子检测到的极低刚度的来源位于蛋白质球状部分的外部。

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《Macromolecular theory and simulations》 |2008年第8期|共9页
作者
Aprodu I; Soncini M; Redaelli A;
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正文语种 eng
中图分类高分子化学（高聚物）;
关键词
kinesin; mechanical properties; molecular dynamics; myosin; MYOSIN SUBFRAGMENT-1; OPTICAL TWEEZERS; MUSCLE; ACTIN; FILAMENTS; FORCE; EXTENSIBILITY; BIOMOLECULES; SIMULATIONS; ELASTICITY;

机译：驱动蛋白;力学性能;分子动力学;肌球蛋白;肌球蛋白亚片段-1;光学镊子;肌肉;肌动蛋白;细丝;力;可扩展性;生物分子;模拟;弹性;

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Mechanical Characterization of Motor Proteins: A Molecular Dynamics Approach

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