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血影蛋白自缔合热力学的重新研究。

Reinvestigation of the thermodynamics of spectrin self-association.

作者信息

Henniker A, Ralston G B

机构信息

Department of Biochemistry, University of Sydney, NSW, Australia.

出版信息

Biophys Chem. 1994 Nov;52(3):251-8. doi: 10.1016/0301-4622(94)00094-z.

Abstract

The thermodynamics of the self-association reactions of human spectrin have been reinvestigated by means of sedimentation equilibrium over the temperature range 18-40 degrees C. The experimental data were analysed in terms of a cooperative isodesmic model of association. The van't Hoff plot showed that the standard change in enthalpy for the heterodimer-tetramer step was temperature-dependent, leading to an estimate of -8.5 kJ mol-1 K-1 for the change in molar heat capacity, delta Cp. Curvature in the van't Hoff plots, not detected in previous studies, was revealed through the increased precision of the data and the wider temperature range examined. On the assumption that delta Cp reflects hydrophobic interactions in the tetramer that cannot be formed in the heterodimer, it can be estimated that approximately 50 CH2 groups per heterodimer participate in hydrophobic interactions in the tetramer that cannot be formed in the heterodimer.

摘要

通过沉降平衡法,在18 - 40摄氏度的温度范围内,对人血影蛋白自缔合反应的热力学进行了重新研究。依据缔合的协同等键模型对实验数据进行了分析。范特霍夫图表明,异二聚体 - 四聚体步骤的标准焓变与温度有关,由此估计摩尔热容变化量ΔCp为 - 8.5 kJ mol⁻¹ K⁻¹。通过提高数据精度和扩大研究的温度范围,揭示了先前研究中未检测到的范特霍夫图中的曲率。假设ΔCp反映了四聚体中异二聚体无法形成的疏水相互作用,则可以估计每个异二聚体中约有50个CH₂基团参与了异二聚体无法形成的四聚体中的疏水相互作用。

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