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Studies of the diffuse x-ray scattering from contracting frog skeletal muscles.对收缩中的青蛙骨骼肌的漫射X射线散射的研究。
Biophys J. 1990 May;57(5):977-85. doi: 10.1016/S0006-3495(90)82617-5.
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X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles.对去表皮兔腰大肌肌球蛋白头部有序-无序转变的X射线研究。
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X-ray study of myosin heads in contracting frog skeletal muscle.收缩的青蛙骨骼肌中肌球蛋白头部的X射线研究。
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Intensity changes of actin-based layer lines from frog skeletal muscles during an isometric contraction.青蛙骨骼肌等长收缩过程中基于肌动蛋白的层线强度变化。
Adv Exp Med Biol. 1988;226:353-67.
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Cause of changes in the thin filament-associated reflexions on activation of frog muscle--myosin binding or conformational change of actin.青蛙肌肉激活时细肌丝相关反射变化的原因——肌球蛋白结合还是肌动蛋白的构象变化。
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An X-ray diffraction study of frog skeletal muscle during shortening near the maximum velocity.对青蛙骨骼肌在接近最大速度缩短过程中的X射线衍射研究。
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X-ray evidence that in contracting live frog muscles there exist two distinct populations of myosin heads.X光证据表明,在收缩的活蛙肌肉中存在两种不同类型的肌球蛋白头部群体。
Biophys J. 1995 Apr;68(4 Suppl):99S-104S; discussion 104S-105S.

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Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog.青蛙骨骼肌纤维中肌球蛋白丝结构的肌节长度依赖性
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Birefringence changes associated with isometric contraction and rapid shortening steps in frog skeletal muscle fibres.与青蛙骨骼肌纤维等长收缩和快速缩短步骤相关的双折射变化。
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X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles.对去表皮兔腰大肌肌球蛋白头部有序-无序转变的X射线研究。
Biophys J. 1991 Oct;60(4):812-24. doi: 10.1016/S0006-3495(91)82116-6.
8
Myosin step size: estimates from motility assays and shortening muscle.肌球蛋白步长:来自运动分析和肌肉收缩的估计值。
J Muscle Res Cell Motil. 1992 Dec;13(6):590-607. doi: 10.1007/BF01738249.

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Time-resolved X-ray diffraction studies of the structural behaviour of myosin heads in a living contracting unstriated muscle.对活的收缩性无横纹肌中肌球蛋白头部结构行为的时间分辨X射线衍射研究。
Nature. 1982 Sep 23;299(5881):308-12. doi: 10.1038/299308a0.
2
Time-resolved X-ray diffraction studies of the myosin layer-line reflections during muscle contraction.肌肉收缩过程中肌球蛋白层线反射的时间分辨X射线衍射研究。
J Mol Biol. 1982 Jul 15;158(4):637-84. doi: 10.1016/0022-2836(82)90253-4.
3
A model of myosin crossbridge structure consistent with the low-angle x-ray diffraction pattern of vertebrate muscle.一种与脊椎动物肌肉的低角度X射线衍射图谱相符的肌球蛋白横桥结构模型。
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Structure of myosin/paramyosin filaments from a molluscan smooth muscle.来自软体动物平滑肌的肌球蛋白/副肌球蛋白丝的结构。
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Small-angle X-ray scattering from myosin heads in relaxed and rigor frog skeletal muscles.来自松弛和僵直状态青蛙骨骼肌中肌球蛋白头部的小角X射线散射。
Nature. 1983;303(5913):146-52. doi: 10.1038/303146a0.
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Changes in the X-ray reflections from contracting muscle during rapid mechanical transients and their structural implications.快速机械瞬变期间收缩肌肉的X射线反射变化及其结构意义。
J Mol Biol. 1983 Sep 15;169(2):469-506. doi: 10.1016/s0022-2836(83)80062-x.
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Structure of the myosin projections on native thick filaments from vertebrate skeletal muscle.脊椎动物骨骼肌天然粗肌丝上肌球蛋白突起的结构。
J Mol Biol. 1984 Aug 15;177(3):461-82. doi: 10.1016/0022-2836(84)90295-x.
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Orientation of spin-labeled myosin heads in glycerinated muscle fibers.甘油化肌纤维中自旋标记肌球蛋白头部的取向
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The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor.脊椎动物横纹肌的低角度X射线图及其在收缩和强直过程中的表现。
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Myosin filaments in vertebrate smooth muscle.脊椎动物平滑肌中的肌球蛋白丝。
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对收缩中的青蛙骨骼肌的漫射X射线散射的研究。

Studies of the diffuse x-ray scattering from contracting frog skeletal muscles.

作者信息

Lowy J, Poulsen F R

机构信息

Open University Research Unit, Oxford, United Kingdom.

出版信息

Biophys J. 1990 May;57(5):977-85. doi: 10.1016/S0006-3495(90)82617-5.

DOI:10.1016/S0006-3495(90)82617-5
PMID:2340345
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1280804/
Abstract

Using x-rays from synchrotron radiation, we studied diffuse scattering, sometimes together with the myosin layer lines. With an area detector, sartorius muscles and a time resolution of 150 ms, earlier results from semitendinosus muscles contracting isometrically at 6 degrees C (Lowy, J., and F. R. Poulsen. 1987. J. Mol. Biol. 194:595-600) were confirmed and extended. Evidence from intensity changes both in the diffuse scattering and in the myosin layer lines showed that the majority of the heads become disordered at peak tetanic tension. With a linear detector and a time resolution of 5 ms, it was found that during tension rise the intensity increase of the diffuse scattering (which amounted maximally to 12% recorded near the meridian) runs approximately 20 ms ahead of the mechanical change, comparing half-completion times. This suggests that an appreciable number of heads change orientation before peak tension is reached. In quick release experiments the diffuse scattering intensity showed very little change. Recorded near the meridian during rapid shortening, however, it decreased progressively with a half-time of approximately 40 ms. This change amounted to approximately 35% of that observed during the initial tension rise. We interpret this to indicate that during rapid shortening a certain number of heads assume an orientation characteristic of the relaxed state. Viewed in the context of the behavior of the first myosin layer line and the (1, 1) equatorial reflection in similar experiments (Huxley, H. E., M. Kress, A. R. Faruqi, and R. M. Simmons. 1988. Molecular Mechanism of Muscle Contraction), the present results provide further support for the view that the diffuse scattering is mostly due to disordered myosin heads; whilst ordered heads produce the myosin layer lines (Poulsen, F. R., and J. Lowy.1983. Nature lLond.l. 303:146-152).

摘要

利用同步辐射产生的X射线,我们研究了漫散射,有时还结合肌球蛋白层线进行研究。使用面积探测器、缝匠肌以及150毫秒的时间分辨率,对半腱肌在6摄氏度下等长收缩的早期研究结果(Lowy, J., and F. R. Poulsen. 1987. J. Mol. Biol. 194:595 - 600)得到了证实和扩展。漫散射和肌球蛋白层线强度变化的证据表明,在强直收缩张力峰值时,大多数头部变得无序。使用线性探测器和5毫秒的时间分辨率发现,在张力上升过程中,漫散射强度的增加(在子午线附近记录到的最大增加量为12%)在比较半完成时间时,比机械变化提前约20毫秒。这表明在达到张力峰值之前,相当数量的头部会改变方向。在快速释放实验中,漫散射强度变化很小。然而,在快速缩短过程中于子午线附近记录时,它以约40毫秒的半衰期逐渐下降。这种变化量约为初始张力上升期间观察到的变化量的35%。我们将此解释为表明在快速缩短过程中,一定数量的头部呈现出松弛状态的特征取向。从类似实验中第一条肌球蛋白层线和(1, 1)赤道反射的行为背景来看(Huxley, H. E., M. Kress, A. R. Faruqi, and R. M. Simmons. 1988. Molecular Mechanism of Muscle Contraction),目前的结果进一步支持了这样一种观点,即漫散射主要是由于无序的肌球蛋白头部引起的;而有序的头部产生肌球蛋白层线(Poulsen, F. R., and J. Lowy.1983. Nature lLond.l. 303:146 - 152)。