Dynamical and temperature-dependent effects of lipid-protein interactions. Application of deuterium nuclear magnetic resonance and electron paramagnetic resonance spectroscopy to the same reconstitutions of cytochrome c oxidase.
Dynamical and temperature-dependent effects of lipid-protein interactions. Application of deuterium nuclear magnetic resonance and electron paramagnetic resonance spectroscopy to the same reconstitutions of cytochrome c oxidase.
复制标题
脂质-蛋白质相互作用的动力学和温度依赖性效应。
DOI：
10.1021/bi00514a026
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Bloom,M
中科院分区：
文献类型：
--
作者：
Paddy,MR;Dahlquist,FW;Davis,JH;Bloom,M
Michael R. Paddy, F. W. Dahlquist,* James H. Davis, 1 和 Myer Bloom 摘要：从重构为 1-(16, 16, 16-三氘代棕榈油酰基)-2-棕榈油酰基-jzi-甘油-3-磷酸胆碱。在所有温度下，EPR 谱都显示出特征“结合”和“游离”成分，而 2H NMR 谱仅显示取向有序参数的狭窄分布。在接近纯脂质相变的温度下，2H NMR 平均取向顺序对蛋白质浓度的依赖性符合二态模型，其中磷脂分子在初步确定为蛋白质表面上或蛋白质表面外位点的两种状态之间快速交换。根据该模型，2 H NMR 光谱得出每毫克蛋白质需要 0.18 毫克磷脂的值，以覆盖细胞色素 C 氧化酶的表面，该值与 20°C 时的 EPR 光谱得出的值相同。2 H NMR 和 EPR 光谱均随温度而显着变化。在
Michael R. Paddy, F. W. Dahlquist,* James H. Davis, 1 and Myer Bloom abstract: 2H NMR and EPR spectra have been obtained as a function of temperature and protein concentration from the same samples of beef heartmitochondrial cytochrome c oxidase reconstituted into 1-(16, 16, 16-trideuteriopalmit-oyl)-2-palmitoleoyl-jzi-glycero-3-phosphocholine. At all temperatures, the EPR spectra show the characteristic “bound” and “free” components, while the 2H NMR spectra show only a narrow distribution of orientationalorder parameters. At temperatures near the phase transition of the pure lipid, the dependence of the 2H NMR average orientational order on protein concentration fits a two-state model in which the phospholipid molecules exchange rapidly between two states tentatively identified as sites either on or off the protein surface. From this model, the 2H NMR spectra yield a value of 0.18 mg of phospholipid per mg of protein as necessary to cover the surface of cytochrome c oxidase, which is the same value as derived from the EPR spectra at-20 C. Both the2H NMR and EPR spectra vary markedly with temperature. At