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螺旋阵列中偶极探针的三维无序。在肌肉横桥中的应用。

Three-dimensional disorder of dipolar probes in a helical array. Application to muscle cross-bridges.

作者信息

Mendelson R A, Wilson M G

出版信息

Biophys J. 1982 Aug;39(2):221-7. doi: 10.1016/S0006-3495(82)84511-6.

DOI:10.1016/S0006-3495(82)84511-6
PMID:6288134
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1328935/
Abstract

Fluorescence polarization and EPR experiments on azimuthally randomized helices bearing extrinsic (dipolar) probes yield information about the axial orientation and order of the probes. If the orientation of the probe on the structure bearing it is known and disorder is absent, the orientation of the structure may be ascertained. For cases where less probe orientation information is available and/or disorder is present, the available structural information is correspondingly reduced. Here we examine the available data on probes attached to cross-bridges in muscle fibers: four plausible cases of three-dimensional cross-bridge disorders are numerically modeled muscle in states of rigor and relaxation. In rigor, where the reported probe disorder is small (Thomas and Cooke, 1980), it was found that the cross-bridge disorder was also small. On the other hand, for the relaxed state where the probes are found to be completely disordered, the cross-bridges may have a considerable amount of order. This possibility is in concert with the results of x-ray diffraction, in which the presence of well-developed myosin-based layer lines indicates considerable order in relaxed muscle.

摘要

对带有外在(偶极)探针的方位随机螺旋进行荧光偏振和电子顺磁共振实验,可得出有关探针轴向取向和排列顺序的信息。如果已知探针在承载它的结构上的取向且不存在无序情况,则可以确定该结构的取向。对于探针取向信息较少和/或存在无序的情况,可用的结构信息相应减少。在这里,我们研究了附着在肌纤维横桥上的探针的现有数据:对三种三维横桥无序的合理情况进行了数值模拟,模拟了处于强直和松弛状态的肌肉。在强直状态下,据报道探针的无序程度较小(托马斯和库克,1980年),发现横桥的无序程度也较小。另一方面,对于发现探针完全无序的松弛状态,横桥可能具有相当程度的有序性。这种可能性与X射线衍射结果一致,在X射线衍射中,发达的基于肌球蛋白的层线的存在表明松弛肌肉中存在相当程度的有序性。

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本文引用的文献

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Polarization from a helix of fluorophores and its relation to that obtained from muscle.来自荧光团螺旋的偏振及其与从肌肉获得的偏振的关系。
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Stress does not alter the conformation of a domain of the myosin cross-bridge in rigor muscle fibres.应激不会改变强直收缩肌纤维中肌球蛋白横桥结构域的构象。
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Angles of nucleotides bound to cross-bridges in glycerinated muscle fiber at various concentrations of epsilon-ATP, epsilon-ADP and epsilon-AMPPNP detected by polarized fluorescence.通过偏振荧光检测在不同浓度的ε-ATP、ε-ADP和ε-AMPPNP下甘油化肌纤维中与横桥结合的核苷酸的角度。
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