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首页> 外文期刊>Nature Communications >Structural dynamics in proteins induced by and probed with X-ray free-electron laser pulses
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Structural dynamics in proteins induced by and probed with X-ray free-electron laser pulses

机译：用X射线自由电子激光脉冲诱导和探测蛋白质中的结构动力学

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X-ray free-electron lasers (XFELs) enable crystallographic structure determination beyond the limitations imposed upon synchrotron measurements by radiation damage. The need for very short XFEL pulses is relieved through gating of Bragg diffraction by loss of crystalline order as damage progresses, but not if ionization events are spatially non-uniform due to underlying elemental distributions, as in biological samples. Indeed, correlated movements of iron and sulfur ions were observed in XFEL-irradiated ferredoxin microcrystals using unusually long pulses of 80?fs. Here, we report a femtosecond time-resolved X-ray pump/X-ray probe experiment on protein nanocrystals. We observe changes in the protein backbone and aromatic residues as well as disulfide bridges. Simulations show that the latter's correlated structural dynamics are much slower than expected for the predicted high atomic charge states due to significant impact of ion caging and plasma electron screening. This indicates that dense-environment effects can strongly affect local radiation damage-induced structural dynamics.
机译：X射线自由电子激光器（XFELS）使得晶体结构确定超出通过辐射损伤对同步测量施加的限制的限制。通过损失的晶体顺序作为损坏进展而丧失晶体顺序的Bragg衍射的衍生来缓解了对非常短的XFEL脉冲的需求，但由于在生物样品中，电离事件由于电离事件是空间而不是均匀的。实际上，使用异常长的80°FS的XFEL辐照的富勒霉蛋白微晶，在XFEL辐照的富勒霉蛋白微晶中观察到熨斗和硫离子的相关运动。在这里，我们在蛋白质纳米晶体上报告了一只飞秒时间分辨的X射线泵/ X射线探测试验。我们观察蛋白质骨干和芳族残留物以及二硫化物桥的变化。模拟表明，由于离子捕获和等离子体电子筛选的显着影响，后者的相关结构动力学比预测的高原子充电状态要慢得多。这表明密集环境效应能够强烈影响局部辐射损伤诱导的结构动态。

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