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首页> 外文期刊>Journal of Molecular Biology >New X-ray Diffraction Observations on Vertebrate Muscle: Organisation of C-protein (MyBP-C) and Troponin and Evidence for Unknown Structures in the Vertebrate A-band.
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New X-ray Diffraction Observations on Vertebrate Muscle: Organisation of C-protein (MyBP-C) and Troponin and Evidence for Unknown Structures in the Vertebrate A-band.

机译：脊椎动物肌肉的新X射线衍射观察：C蛋白（MyBP-C）和肌钙蛋白的组织以及脊椎动物A波段中未知结构的证据。

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Previous low-angle X-ray diffraction studies of various vertebrate skeletal muscles have shown the presence of two rich layer-line patterns, one from the myosin heads and based on a 429A axial repeat, and one from actin filaments and based on a repeat of about 360-370A. In addition, meridional intensities have been seen from C-protein (MyBP-C; at about 440A and its higher orders) and troponin (at about 385A and its orders). Using preparations of intact, relaxed, bony fish fin muscles and the ID-02 low-angle X-ray camera at the ESRF with a 10m camera length we have now seen numerous, hitherto unreported, sampled, X-ray layer-lines many of which do not fit onto the previously observed repeats and which require interpretation. The new reflections all fall on the normal ("vertical") hexagonal lattice row-lines in the highly sampled, almost "crystalline", low-angle diffraction X-ray patterns from bony fish muscle, indicating that they all arise from the muscle A-band. However, they do not fall on a single axial repeat. In direct confirmation of our previous analysis, some of these new reflections are explained by the interaction in resting muscle between the N-terminal ends of myosin-bound C-protein molecules with adjacent actin filaments, possibly through the Pro-Ala-rich region. Other newly observed reflections lie on a much longer repeat, but they are most easily interpreted in terms of the arrangement of troponin on the actin filaments. If this is so, then the implication is that the actin filaments and their troponin complexes are systematically arranged in the fish muscle A-band lattice relative to the myosin head positions, and that these newly observed X-ray reflections, when fully analysed, will report on the shape and distribution of troponin molecules in the resting muscle A-band. The less certain contributions of titin and nebulin to these new reflections have also been tested and are described. Many of the new reflections do not appear to come from these known structures. There must be structural features of the A-band that have not yet been described.
机译：先前对各种脊椎动物骨骼肌进行的低角度X射线衍射研究表明，存在两种丰富的层线模式，一种来自肌球蛋白头部，基于429A轴向重复，另一种来自肌动蛋白丝，基于重复约360-370A。此外，从C蛋白（MyBP-C;约440A及其更高阶数）和肌钙蛋白（约385A及其阶数）中发现子午线强度。在ESRF上使用完整，放松的骨状鱼鳍肌肉和ID-02低角度X射线照相机的准备，照相机长度为10m，我们现在已经看到许多迄今未报告，采样过的X射线分层线，不适合先前观察到的重复，需要解释。新反射全部落在来自骨骼鱼肌肉的高度采样的，几乎“晶状”的低角度衍射X射线图的法线（“垂直”）六角形格子行线上，表明它们全部来自于肌肉A -带。但是，它们不会落在单个轴向重复上。在直接确认我们先前的分析后，其中一些新的反映是由肌球蛋白结合的C蛋白分子的N末端与邻近的肌动蛋白丝之间的静息肌之间的相互作用所解释的，可能是通过富含Pro-Ala的区域。其他新近观察到的反射出现在更长的重复上，但就肌动蛋白丝上肌钙蛋白的排列而言，最容易解释。如果是这样的话，则意味着肌动蛋白丝及其肌钙蛋白复合物相对于肌球蛋白的头部位置被系统地排列在鱼肌的A波段晶格中，并且在充分分析后，这些新近观察到的X射线反射将肌钙蛋白分子在静息肌A波段的形状和分布的报告。 titin和nebulin对这些新反射的不确定性贡献也已得到测试和描述。许多新的反射似乎并不来自这些已知的结构。必须具有尚未描述的A波段结构特征。

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