三脉冲光子回波峰移光谱法作为探测蛋白质折叠中灵活性和构象异质性的手段
Three-pulse photon echo peak shift spectroscopy as a probe of flexibility and conformational heterogeneity in protein folding.
作者信息
Gibson Emily A, Shen Zhaochuan, Jimenez Ralph
机构信息
Department of Physics, University of Colorado Denver, Denver, CO 80217, USA.
出版信息
Chem Phys Lett. 2009 Jan 1;473(4-6):330-335. doi: 10.1016/j.cplett.2009.04.002.
We investigate the equilibrium unfolding of Zn-cytochrome c in guanidine hydrochloride by three-pulse photon echo peak shift (3PEPS) spectroscopy. Unexpectedly, the measurements reveal that inhomogeneous broadening of the sample at the midpoint of the denaturation is larger than that of either native or unfolded states. To interpret this finding, we present simulations of the peak shift for both two-state and three-state unfolding models. Both the denaturant concentration dependence of the asymptotic peak shift (APS) and the wavelength dependence of the APS at the midpoint of the denaturation are different for the two models. Our data are consistent with two-state unfolding.
我们通过三脉冲光子回波峰移（3PEPS）光谱研究了盐酸胍中锌细胞色素c的平衡去折叠。出乎意料的是，测量结果表明，在变性中点处样品的非均匀展宽大于天然态或去折叠态。为了解释这一发现，我们给出了两态和三态去折叠模型的峰移模拟。两种模型的渐近峰移（APS）的变性剂浓度依赖性以及变性中点处APS的波长依赖性均不同。我们的数据与两态去折叠一致。
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