变性剂m值和热容变化：与蛋白质展开时可及表面积变化的关系。
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding.
作者信息
Myers J K, Pace C N, Scholtz J M
机构信息
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843, USA.
出版信息
Protein Sci. 1995 Oct;4(10):2138-48. doi: 10.1002/pro.5560041020.
Abstract
Denaturant m values, the dependence of the free energy of unfolding on denaturant concentration, have been collected for a large set of proteins. The m value correlates very strongly with the amount of protein surface exposed to solvent upon unfolding, with linear correlation coefficients of R = 0.84 for urea and R = 0.87 for guanidine hydrochloride. These correlations improve to R = 0.90 when the effect of disulfide bonds on the accessible area of the unfolded protein is included. A similar dependence on accessible surface area has been found previously for the heat capacity change (delta Cp), which is confirmed here for our set of proteins. Denaturant m values and heat capacity changes also correlate well with each other. For proteins that undergo a simple two-state unfolding mechanism, the amount of surface exposed to solvent upon unfolding is a main structural determinant for both m values and delta Cp.
摘要
已经收集了大量蛋白质的变性剂m值，即去折叠自由能对变性剂浓度的依赖性。m值与蛋白质去折叠时暴露于溶剂的表面积密切相关，对于尿素，线性相关系数R = 0.84，对于盐酸胍，R = 0.87。当考虑二硫键对去折叠蛋白质可及面积的影响时，这些相关性提高到R = 0.90。先前已经发现热容变化（ΔCp）对可及表面积有类似的依赖性，本文对我们的蛋白质组也证实了这一点。变性剂m值和热容变化之间也有很好的相关性。对于经历简单两态去折叠机制的蛋白质，去折叠时暴露于溶剂的表面积是m值和ΔCp的主要结构决定因素。
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