Single-molecule tracking of sub-millisecond domain motion in calmodulin.
Single-molecule tracking of sub-millisecond domain motion in calmodulin.
复制标题
钙调蛋白中亚毫秒域运动的单分子跟踪。
DOI：
10.1021/jp051666o
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Johnson,CareyK
中科院分区：
文献类型：
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作者：
Slaughter,BrianD;Bieber-Urbauer,RamonaJ;Johnson,CareyK
我们使用单对荧光共振能量转移（spFRET）跟踪荧光标记的钙调素（CaM）的亚毫秒时间尺度上的域之间的距离变化。在大多数情况下，钙调素保持在相同的构象亚状态超过1毫秒的时间段，表明构象交换发生在一个较长的时间尺度。然而，在某些情况下，可以检测到构象亚状态之间的明显转变。亚毫秒运动的幅度内占主导地位的构象亚状态也揭示了依赖于pH值和离子强度的域之间的距离波动。
We used single-pair fluorescence resonance energy transfer (spFRET) to track distance changes between domains of fluorescently labeled calmodulin (CaM) on the sub-millisecond time scale. In most cases, CaM remained in the same conformational substate over time periods of up to 1 ms, showing that conformational interchange occurs on a longer time scale. However, in some instances, apparent transitions between conformational substates could be detected. The magnitude of sub-millisecond motion within the dominant conformational substate also revealed fluctuations in distance between domains that were dependent on pH and ionic strength.