Bialek W, Goldstein R F
Biophys J. 1985 Dec;48(6):1027-44. doi: 10.1016/S0006-3495(85)83865-0.
We develop a quasi-harmonic description of protein dynamics and apply this description to the anomalous Mössbauer, infrared, x-ray diffraction, and EXAFS (extended x-ray absorption fine structure spectroscopy) data that are available for myoglobin (Mb) and its interactions with carbon monoxide (CO). In the quasi-harmonic approximation the dynamical parameters derived from these spectroscopic data are relevant in the calculation of reaction rates, and we give a quantitative description of the nonexponential kinetics of Mb-CO binding observed at low temperatures. All these data have previously been interpreted in terms of the more complex conformational substates model for protein dynamics. We point out several problems with this model and propose experiments that can provide detailed tests of the quasi-harmonic theory proposed here.
我们建立了一种蛋白质动力学的准谐描述，并将此描述应用于可获得的关于肌红蛋白（Mb）及其与一氧化碳（CO）相互作用的反常穆斯堡尔谱、红外光谱、X射线衍射和扩展X射线吸收精细结构光谱（EXAFS）数据。在准谐近似中，从这些光谱数据导出的动力学参数与反应速率的计算相关，并且我们对在低温下观察到的Mb-CO结合的非指数动力学给出了定量描述。所有这些数据以前都根据更复杂的蛋白质动力学构象亚态模型进行了解释。我们指出了该模型的几个问题，并提出了可以对此处提出的准谐理论进行详细检验的实验。
