蛋白质热变性前新峰形成机制探讨

蛋白质热变性前新峰是蛋白质热变性过程的共性。通过对蛋白质三级结构特征的理论分析及实验验证的方法，研究了蛋白质热变性前新峰的变化规律，从而揭示了该峰产生的机理。采用ＤＳＣ方法对以不同结构水和十二烷基硫酸钠溶液水合溶菌酶样本进行了研究， 结果表明蛋白质的这种热变性前新峰的存在是由于维持其三级结构的疏水相互作用所造成， 新峰出现的峰温及其焓变与水的结构改变及由此而造成的蛋白质中结合水的含量和结构功能的变化有着直接的关系。

STUDY ON FORMATIVE MECHANISM OF PRETHERMODENATURATIONNEW PEAK OF PROTEIN

The prethermodenaturation new peak of protein is the general characteristics in the process of thermodenaturation of protein. In this paper, change of prethermodenaturation new peak of protein was studied through theoretical analysis of tertiary structure of protein and experimental verification,to investigate the mechanism of peak formation was shown. Several samples of lysozyme,hydrated with different structured waters and sodium dodecyl sulfate (SDS) respectively, were investigated by differential scanning calorimetry (DSC). The results showed that the appearance of the prethermodenaturation new peak is resulted from hydrophobic interaction which maintained tertiary structure of protein,and its thermodenaturation temperature and enthalpy change were directly related to water microstructure and changes on structure and amount of bound water arising therefrom in the protein.