BINDING OF MOLTEN GLOBULE-LIKE CONFORMATIONS TO LIPID BILAYERS - STRUCTURE OF NATIVE AND PARTIALLY FOLDED ALPHA-LACTALBUMIN BOUND TO MODEL MEMBRANES
BINDING OF MOLTEN GLOBULE-LIKE CONFORMATIONS TO LIPID BILAYERS - STRUCTURE OF NATIVE AND PARTIALLY FOLDED ALPHA-LACTALBUMIN BOUND TO MODEL MEMBRANES
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DOI：
10.1074/jbc.270.50.29910
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发表时间：
1995-12-15
影响因子：
4.8
通讯作者：
MUGA, A
中科院分区：
文献类型：
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作者：
BANUELOS, S;MUGA, A
通过红外光谱、圆二色性和荧光光谱研究了膜结合对α-乳清蛋白的几种构象异构体的结构和稳定性的影响。在溶液中，在所有构象异构体与带负电荷的膜相互作用的实验条件下，它们表现出显着的构象差异，然而，与带负电荷的膜结合，导致这些构象异构体的结构发生相当大的变化，导致非常相似的蛋白质构象，膜相关构象的特征是1）高螺旋含量，更大与溶液中发现的任何结构相比，2) 缺乏稳定的三级结构，3) 热致转变消失。这些观察结果表明，与带负电的膜结合会诱导 α-乳清蛋白内的构象变化，变为灵活的熔球状状态。
The effect of membrane binding on the structure and stability of several conformers of alpha-lactalbumin was studied by infrared spectroscopy, circular dichroism, and fluorescence spectroscopy, In solution, under experimental conditions where all conformers interact with negatively charged membranes, they show significant conformational differences, However, binding to negatively charged membranes, which causes considerable changes in the structure of these conformers, leads to a remarkably similar protein conformation, The membrane-associated conformations are characterized by 1) a high helical content, greater than any of those found in solution, 2) a lack of stable tertiary structure, and 3) the disappearance of their thermotropic transition, These observations indicate that association with negatively charged membranes induces a conformational change within alpha-lactalbumin to a flexible, molten globule-like state.