压力对蜂毒肽自缔合的影响。
Effect of pressure on the self-association of melittin.
作者信息
Thompson R B, Lakowicz J R
出版信息
Biochemistry. 1984 Jul 17;23(15):3411-7. doi: 10.1021/bi00310a005.
Abstract
The effect of increased hydrostatic pressure (1 bar to 1.8 kbar) on the self-association of melittin was measured by using the fluorescence anisotropy of its single tryptophan residue. The degree of self-association was found to decrease with increasing pressure. The volume change (delta V) for dissociation is surprisingly large. At low pressures, delta V for dissociation is near -150 mL/mol. The magnitude of the volume change decreased with increasing pressure, possibly as a result of pressure-induced compression of free volume trapped at the subunit interface region of the tetramer. Overall, the pressure-dependent association of melittin is comparable to that expected for hydrophobic interactions and to that found for micelle formation by detergents.
摘要
通过测量蜂毒肽单个色氨酸残基的荧光各向异性，研究了静水压力增加（从1巴到1.8千巴）对蜂毒肽自缔合的影响。结果发现，自缔合程度随压力增加而降低。解离的体积变化（ΔV）出奇地大。在低压下，解离的ΔV接近-150 mL/mol。体积变化的幅度随压力增加而减小，这可能是由于压力诱导四聚体亚基界面区域截留的自由体积压缩所致。总体而言，蜂毒肽的压力依赖性缔合与疏水相互作用预期的情况以及洗涤剂形成胶束的情况相当。
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本文引用的文献
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