Fritsch K, Friedrich J, Parak F, Skinner J L
Physikalisches Institut, Universität Bayreuth, Germany.
Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15141-5. doi: 10.1073/pnas.93.26.15141.
We present a novel type of spectral diffusion experiment in the millikelvin range to characterize the energy landscape of a protein as compared with that of a glass. We measure the time evolution of spectral holes for more than 300 hr after well-defined initial nonequilibrium conditions. We show that the model of noninteracting two-level systems can describe spectral diffusion in the glass, but fails for the protein. Our results further demonstrate that randomness in the energy landscape of a protein shows features of organization. There are "deep minimum" states separated by barriers, the heights of which we are able to estimate. The energy landscape of a glass is featureless by comparison.
我们展示了一种新型的毫开尔文温度范围内的光谱扩散实验,用于表征蛋白质与玻璃的能量景观。在明确的初始非平衡条件之后,我们测量了超过300小时的光谱孔时间演化。我们表明,非相互作用两能级系统模型可以描述玻璃中的光谱扩散,但对蛋白质不适用。我们的结果进一步证明,蛋白质能量景观中的随机性呈现出组织特征。存在由势垒分隔的“深最小值”状态,我们能够估计其高度。相比之下,玻璃的能量景观没有特征。