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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Direct observation of fast protein conformational switching
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Direct observation of fast protein conformational switching

机译：直接观察快速蛋白质构象转换

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摘要

Folded proteins can exist in multiple conformational substates. Each substate reflects a local minimum on the free-energy landscape with a distinct structure. By using ultrafast 2D-IR vibrational echo chemical-exchange spectroscopy, conformational switching between two well defined substates of a myoglobin mutant is observed on the ≈ 50-ps time scale. The conformational dynamics are directly measured through the growth of cross peaks in the 2D-IR spectra of CO bound to the heme active site. The conformational switching involves motion of the distal histidine/E helix that changes the location of the imidazole side group of the histidine. The exchange between substates changes the frequency of the CO, which is detected by the time dependence of the 2D-IR vibrational echo spectrum. These results demonstrate that interconversion between protein conformational substates can occur on very fast time scales. The implications for larger structural changes that occur on much longer time scales are discussed.
机译：折叠的蛋白质可以多种构象状态存在。每个子州都以不同的结构反映了自由能景观中的局部最小值。通过使用超快2D-IR振动回波化学交换光谱，可以在约50 ps的时间尺度上观察到肌红蛋白突变体的两个明确定义的亚状态之间的构象转换。构象动力学是通过结合在血红素活性位点上的CO的2D-IR光谱中交叉峰的增长直接测量的。构象转换涉及远端组氨酸/ E螺旋的运动，其改变了组氨酸的咪唑侧基的位置。子状态之间的交换会更改CO的频率，该频率由2D-IR振动回波谱的时间依赖性检测。这些结果表明，蛋白质构象亚状态之间的相互转化可以在非常快的时间尺度上发生。讨论了在更长的时间范围内发生的较大结构变化的含义。

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