Burdzhanadze T V, Bezhitadze M O
Biofizika. 1988 Mar-Apr;33(2):220-5.
Thermodynamic and structural parameters of partially denaturated collagen which had undergone denaturation of different degrees are measured. On the basis of comparative analysis of these data it is established that denaturation enthalpy and secondary structure degree are linearly linked. These investigations made it possible to determine special features of heat absorption curves as well. It is concluded that heat absorption at collagen denaturation must be followed by corresponding conformational alteration.
对经历了不同程度变性的部分变性胶原蛋白的热力学和结构参数进行了测量。在对这些数据进行比较分析的基础上,确定了变性焓和二级结构程度呈线性相关。这些研究也使得确定吸热曲线的特征成为可能。得出的结论是,胶原蛋白变性时的吸热必然伴随着相应的构象改变。