原卟啉IX取代肌红蛋白的光谱烧孔研究
Spectral hole burning study of protoporphyrin IX substituted myoglobin.
作者信息
Zollfrank J, Friedrich J, Parak F
机构信息
Institut für Physikalische Chemie, Johannes Gutenberg-Universität, Mainz, Germany.
出版信息
Biophys J. 1992 Mar;61(3):716-24. doi: 10.1016/S0006-3495(92)81876-3.
Abstract
Protoporphyrin IX substituted myoglobin reveals excellent hole burning properties. We investigated the frequency shift of persistent spectral holes under isotropic pressure conditions in a range from 0 to 2.4 MPa. In this range, the protein behaves like an elastic solid. The shift of the holes under pressure shows a remarkable frequency dependence from which the compressibility of the protein can be determined. The compressibility, in turn, allows for an estimation of the equilibrium volume fluctuations. Within the frame of the model used to interpret the pressure data, it is possible to determine the absorption frequency of the isolated chromophore and the associated solvent shift in the protein environment.
摘要
原卟啉IX取代的肌红蛋白展现出优异的光烧孔特性。我们研究了在0至2.4兆帕的各向同性压力条件下持续光谱孔的频移。在此压力范围内，该蛋白质表现得像弹性固体。压力下孔的频移呈现出显著的频率依赖性，据此可确定蛋白质的压缩性。而压缩性又可用于估算平衡体积涨落。在用于解释压力数据的模型框架内，能够确定孤立发色团的吸收频率以及在蛋白质环境中的相关溶剂位移。
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