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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Cooperative unfolding of apolipoprotein A-1 induced by chemical denaturation
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Cooperative unfolding of apolipoprotein A-1 induced by chemical denaturation

机译：化学变性诱导的载脂蛋白A-1的合作展开

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摘要

Apolipoprotein A-1 (Apo A-1) plays an important role in lipid transfer and obesity. Chemical unfolding of alpha-helical Apo A-1 is induced with guanidineHCl and monitored with differential scanning calorimetry (DSC) and CD spectroscopy. The unfolding enthalpy and the midpoint temperature of unfolding decrease linearly with increasing guanidineHCl concentration, caused by the weak binding of denaturant. At room temperature, binding of 50-60 molecules guanidineHCl leads to a complete Apo A-1 unfolding. The entropy of unfolding decreases to a lesser extent than the unfolding enthalpy. Apo A-1 chemical unfolding is a dynamic multi-state equilibrium that is analysed with the Zimm-Bragg theory modified for chemical unfolding. The chemical Zimm-Bragg theory predicts the denaturant binding constant K-D and the protein cooperativity sigma. Chemical unfolding of Apo A-1 is two orders of magnitude less cooperative than thermal unfolding. The free energy of thermal unfolding is similar to 0.2 kcal/mol per amino acid residue and similar to 1.0 kcal/mol for chemical unfolding at room temperature. The Zimm-Bragg theory calculates conformational probabilities and the chemical Zimm-Bragg theory predicts stretches of alpha-helical segments in dynamic equilibrium, unfolding and refolding independently and fast.
机译：载脂蛋白A-1（APO A-1）在脂质转移和肥胖症中起重要作用。 α-螺旋APO A-1的化学展开诱导胍尼宁HCL，并用差示扫描量热法（DSC）和CD光谱监测。展开焓和展开的中点温度随着变性的弱结合而导致的胍丁尼碱浓度随而导致的。在室温下，50-60分子的结合胍迪宁HCL导致完整的APO A-1展开。展开的熵减少到比展开焓的程度更小。 APO A-1化学展开是一种动态的多状态平衡，随着用于化学展开的Zimm-Bragg理论分析。化学ZIMM-BRAGG理论预测了变性结合常数K-D和蛋白质合作σ。 APO A-1的化学展开是比热展开的两个数量级的数量级。热展开的自由能量与每氨基酸残基相似的0.2kcal / mol，并且类似于在室温下的化学展开的1.0kcal / mol。 Zimm-Bragg理论计算构象概率和化学Zimm-Bragg理论预测动态平衡，展开和快速折叠的α-螺旋区段的延伸。

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