Monolayers of apolipoproteins at the air/water interface
Monolayers of apolipoproteins at the air/water interface
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DOI：
10.1021/jp010714b
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发表时间：
2001-06-21
影响因子：
3.3
通讯作者：
Mas-Oliva, J
中科院分区：
文献类型：
--
作者：
Bolaños-García, VM;Ramos, S;Mas-Oliva, J
对人载脂蛋白All、CIII、E3和AI进行了二级结构预测分析、克服和恢复热变性的蛋白稳定性及其单层物相行为等方面的研究。我们发现预测的二级结构、两相cl-螺旋和热处理后恢复二级蛋白结构的能力之间保持了良好的关系。对每一种载脂蛋白的研究表明，展开过程的平衡特征和等色点的存在表明该过程具有双态特征。采用压力-面积等温线，并使用布鲁斯特角显微镜对沉积在高离子水亚相上的载脂蛋白单层进行直接观察。我们描述了所有这些蛋白质的气/液相转变。载脂蛋白Al和All在高侧压下表现为两个凝聚相之间的相变。提出了这些蛋白质的二级结构模型。
Human apolipoproteins All, CIII, E3, and AI were studied from different points of view: secondary structure prediction analysis, protein stability to overcome and revert thermal denaturation, and phase behavior of their monolayer. We found a well-preserved relationship among the predicted secondary structure, amphipatic cl-helices, and the ability to recover their secondary protein structure after thermal treatment. With each one of the apolipoproteins studied, the equilibrium character of the unfolding process and the presence of isochromatic points suggested a two-state character for the process. Pressure-area isotherms were carried out, as well as direct observations with a Brewster angle microscope of the apolipoproteins monolayers deposited onto a highly ionic water subphase. We described the gas/liquid-phase transition in all of these proteins. The apolipoproteins Al and All present a phase transition between two condensed phases at high lateral pressures. A model of the secondary structure for these proteins is presented.