School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia.
Biophys Chem. 2009 Dec;145(2-3):64-71. doi: 10.1016/j.bpc.2009.09.001. Epub 2009 Sep 11.
A procedure is described for the direct analysis of osmotic pressure data for reversibly dimerizing proteins that makes allowance for effects of thermodynamic nonideality on the statistical-mechanical basis of the potential-of-mean-force between molecules. Detailed consideration is also given to calculation of the magnitudes of the required virial coefficients. After illustration of the approach with analysis of simulated osmotic pressure data, the method is used to obtain dimerization constants from published osmotic pressure data for soybean proteinase inhibitor, hemoglobin and alpha-chymotrypsin.
介绍了一种可直接分析可可逆二聚化蛋白质渗透压数据的方法，该方法考虑了热力学非理想性对分子间平均力势能统计力学基础的影响。还详细考虑了所需维里系数的计算。在用模拟渗透压数据进行分析说明了该方法之后，将该方法用于从已发表的大豆蛋白酶抑制剂、血红蛋白和α-糜蛋白酶的渗透压数据中获取二聚化常数。
