McLean M A, Sligar S G
Beckman Institute for the Advancement of Science and Technology University of Illinois, Urbana 61801, USA.
Biochem Biophys Res Commun. 1995 Oct 4;215(1):316-20. doi: 10.1006/bbrc.1995.2468.
In recent years many studies have been directed toward the elucidation of the interaction mechanisms within protein-protein complexes. One of the best studies protein-protein complexes has been the cytochrome b5 and cytochrome c electron transfer pair. Thermodynamic information about the association process has been obtained through methods which indirectly measure the binding between the proteins. We report here the use of Isothermal Titration Calorimetry to characterize the association of Rat cytochrome b5 and Horse cytochrome c. The association is accompanied by an unfavorable enthalpy change (+1.0 +/-0.1 Kcal/mole) and a large stabilizing change in entropy (33.9 +/-0.6 eu).
近年来，许多研究都致力于阐明蛋白质 - 蛋白质复合物内部的相互作用机制。关于蛋白质 - 蛋白质复合物的最佳研究之一是细胞色素b5和细胞色素c电子传递对。有关缔合过程的热力学信息是通过间接测量蛋白质之间结合的方法获得的。我们在此报告使用等温滴定量热法来表征大鼠细胞色素b5和马细胞色素c的缔合。这种缔合伴随着不利的焓变（+1.0±0.1千卡/摩尔）和熵的大幅稳定变化（33.9±0.6熵单位）。
