Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, FL 32610-0245, USA.
Protein J. 2010 Nov;29(8):617-30. doi: 10.1007/s10930-010-9286-9.
The thermodynamic parameters for six p53 carboxy-terminus peptide fragments as determined by analytical ultracentrifugal analysis were compared over the experimental temperature range of 275-310 K to evaluate the Gibbs free energy change as a function of temperature, ΔG°(T), from 0 to 400 K using our general linear third-order fitting function, ΔG°(T) = α + βT² + γT³. Data obtained at the typical experimental temperature range are not sufficient to accurately describe the variations observed in the oligomerization of these p53 fragments. It is necessary to determine a number of thermodynamic parameters, all of which can be precisely assessed using this general third-order linear fitting function. These are the heat of reaction, innate temperature-invariant enthalpy, compensatory temperatures and the thermodynamic molecular switch occurring at the thermal set point. This methodology can be used to distinguish the characteristic structure and stability of p53 carboxy-terminal fragments or other p53 mutants. It should be used for the thermodynamic characterization of any interacting biological system.
通过分析超速离心分析确定了六个 p53 羧基末端肽片段的热力学参数,在实验温度范围 275-310 K 内进行了比较,以使用我们的通用线性三阶拟合函数评估 Gibbs 自由能随温度的变化,ΔG°(T) = α + βT² + γT³。在典型的实验温度范围内获得的数据不足以准确描述这些 p53 片段的寡聚化所观察到的变化。有必要确定许多热力学参数,所有这些参数都可以使用这种通用的三阶线性拟合函数来精确评估。这些参数是反应热、内在温度不变焓、补偿温度和在热设定点发生的热力学分子开关。这种方法可用于区分 p53 羧基末端片段或其他 p53 突变体的特征结构和稳定性。它应该用于任何相互作用的生物系统的热力学表征。