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首页> 外文期刊>Journal of Molecular Biology >MICROSECOND ROTATIONAL DYNAMICS OF ACTIN - SPECTROSCOPIC DETECTION AND THEORETICAL SIMULATION
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MICROSECOND ROTATIONAL DYNAMICS OF ACTIN - SPECTROSCOPIC DETECTION AND THEORETICAL SIMULATION

机译：肌动蛋白光谱检测的微观旋转动力学及其理论模拟。

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We have investigated the microsecond rotational dynamics of F-actin with transient phosphorescence anisotropy (TPA) spectroscopy, and analyzed the data to determine the relative contributions from rigid-body rotations and from intrafilament bending and twisting, using a theoretical model developed for DNA dynamics by Schurr and co-workers. The fits of the data to the model were constrained by independently determining the orientation of the dye's absorption dipole (by transient absorption anisotropy, TAA) and the actin filament length distribution (by electron microscopy). We conclude that (1) the Schurr theory enables calculation of the torsional flexibility of actin independent of any contribution from rigid body rotations of the whole filament, (2) the TPA decays cannot be explained by rigid-body or bending rotations, but reflect primarily twisting motions within actin filaments, and (3) the dynamic properties of actin filaments are best ascribed to a continuous elasticity. This analysis establishes a firm methodological foundation for future studies of the effects of perturbations of the dynamics of actin on its functional properties. (C) 1996 Academic Press Limited [References: 45]
机译：我们使用瞬态磷光各向异性（TPA）光谱研究了F-肌动蛋白的微秒旋转动力学，并使用针对DNA动力学的理论模型开发了分析数据，以确定刚体旋转以及丝内弯曲和扭曲的相对贡献。舒尔和同事们。通过独立确定染料吸收偶极子的方向（通过瞬态吸收各向异性，TAA）和肌动蛋白丝长度分布（通过电子显微镜）来限制数据与模型的拟合。我们得出的结论是：（1）Schurr理论使肌动蛋白的扭转柔性计算不受整个丝的刚体旋转的任何影响;（2）TPA衰减不能用刚体或弯曲旋转来解释，而是主要反映出来的。 （3）肌动蛋白丝的动态特性最好归因于连续弹性。该分析为进一步研究肌动蛋白动力学对其功能特性的影响奠定了坚实的方法论基础。 （C）1996 Academic Press Limited [参考号：45]

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