FOLLOWING PROTEIN-FOLDING IN REAL-TIME USING NMR-SPECTROSCOPY
FOLLOWING PROTEIN-FOLDING IN REAL-TIME USING NMR-SPECTROSCOPY
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DOI：
10.1038/nsb1095-865
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发表时间：
1995-10-01
期刊：
影响因子：
--
通讯作者：
DOBSON, CM
中科院分区：
文献类型：
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作者：
BALBACH, J;FORGE, V;DOBSON, CM
在化学变性状态的快速原位稀释之后，通过NMR光谱学在真实的时间内监测了载脂蛋白牛α-乳清蛋白的重折叠。通过检查在时间分辨的NMR光谱中的个别共振，已被证明的天然状态出现在一个合作的方式从形成在实验的死时间的中间体。折叠到天然状态的动力学与通过停流荧光和近紫外圆二色性观察到的动力学非常相似。的瞬态中间体的NMR光谱类似于密切的特点，以及在低pH值下形成的稳定的熔融球状态。结果表明，NMR可以发挥关键作用，在原子水平上描述蛋白质折叠过程中发生的结构转变。
The refolding of apo bovine a-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative manner from an intermediate formed in the dead-time of the experiments. The kinetics of folding to the native state are closely similar to those observed by stopped-flow fluorescence and near-UV circular dichroism. The NMR spectrum of the transient intermediate resembles closely that of the well characterized stable molten globule state formed at low pH. The results suggest that NMR can play a key role in describing at an atomic level the structural transitions occurring during protein folding.