Large-scale rotational motions of proteins detected by electron paramagnetic resonance and fluorescence.
Large-scale rotational motions of proteins detected by electron paramagnetic resonance and fluorescence.
复制标题
通过电子顺磁共振和荧光检测蛋白质的大规模旋转运动。
DOI：
10.1016/s0006-3495(78)85394-6
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发表时间：
1978
影响因子：
3.4
通讯作者：
D. D. Thomas
中科院分区：
文献类型：
--
作者：
D. D. Thomas
蛋白质和大蛋白质片段旋转运动的直接光谱测量对于理解蛋白质功能的分子动力学至关重要。荧光探针和自旋标签附着在蛋白质上已被证明是研究大规模蛋白质运动的有力工具。荧光去极化和常规电子顺磁共振（EPR）适用于纳秒到微秒时间范围内旋转运动的研究，并已被用于证明抗体和肌球蛋白的节段灵活性。非常缓慢的旋转运动，发生在微秒到毫秒的时间范围内，在超分子组装中尤为重要，在超分子组装中，蛋白质的运动受到与其他分子结合的限制。饱和转移光谱（ST-EPR）是一种最近开发的电子顺磁共振（EPR）技术，允许检测旋转相关时间长达1ms，已被用于检测肌肉细丝和膜中自旋标记蛋白质的大规模旋转运动，为这些组件中的能量转导机制提供了有价值的见解。
Direct spectroscopic measurements of rotational motions of proteins and large protein segments are crucial to understanding the molecular dynamics of protein function. Fluorescent probes and spin labels attached to proteins have proved to be powerful tools in the study of large-scale protein motions. Fluorescence depolarization and conventional electron paramagnetic resonance (EPR) are applicable to the study of rotational motions in the nanosecond-to-microsecond time range, and have been used to demonstrate segmental flexibility in an antibody and in myosin. Very slow rotational motions, occurring in the microsecond-to-millisecond time range, are particularly important in supramolecular assemblies, where protein motions are restricted by association with other molecules. Saturation transfer spectroscopy (ST-EPR), a recently developed electron paramagnetic resonance (EPR) technique that permits the detection of rotational correlation times as long as 1 ms, has been used to detect large-scale rotational motions of spin-labeled proteins in muscle filaments and in membranes, providing valuable insights into energy transduction mechanisms in these assemblies.