Denatured Thermodynamics of Proteins in Weak Cation-exchange Chromatography

The thermostability of some proteins in weak cation-exchange chromatography was investigated at 20-80 ℃. The results show that there is a fixed thermal denaturation transition temperature for each protein. The appearance of the thermal transition temperature indicates that the conformations of the proteins are destroyed seriously. The thermal behavior of the proteins in weak cation-exchange and hydrophobic interaction chromatographies were compared in a wide temperature range. It was found that the proteins have a higher thermostability in a weak cation-exchange chromatography system. The thermodynamic parameters(Δ H 0, Δ S 0) of those proteins were determined by means of Vant Hoff relationship(ln k -1/ T ). According to standard entropy change(Δ S 0), the conformational change of the proteins was judged in the chromatographic process. The linear relationships between Δ H 0 and Δ S 0 can be used to evaluate 'compensation temperature'( β ) at the protein denaturation and identify the identity of the protein retention mechanism in weak cation-exchange chromatography.

蛋白质折迭的不可逆热力学理论及蛋白质动态热力学结构(英文)

在机械力学及热力学基础上阐述蛋白质的各种物理性质是从物理学角度理解生物学的基础性工作 .详细讨论了蛋白质折迭的不可逆热力学理论 ,蛋白质动态热力学结构理论 .理论推断蛋白质动态热力学变化是一切生物学状态变化的基本热力学状态单位并作为分子生物学变化的分子开关 .利用此理论解释了蛋白质的物理学性质及麻醉药的生物物理学机制 .

蛋白质折迭的若干物理问题

综述了蛋白质折迭的基本实验特征，讨论了量子构象动力学的有关理论结果，分析了格子模拟得到的启示，在此基础上对Ａｎｆｉｎｓｅｎ的热力学假设提出质疑，提出鲁棒极小值的概念，研究了序列决定构象（第二遗传密码）问题，并对折迭途径中的一些问题进行了初步探讨。

蛋白界面膜及其评价方法研究进展

食品中乳化类产品的稳定性决定了其价值和顾客满意度,天然蛋白的乳化特性多年来受到食品胶体和界面科学领域广泛关注。蛋白吸附到水油界面形成的黏弹性薄膜具有降低界面张力、维持乳液稳定的特性。研究蛋白界面膜的物化性质有助于了解蛋白大分子在水油界面的吸附规律,能够用于评价、表征和预测蛋白乳液稳定性,并为优化蛋白乳液稳定性提供理论基础。基于此,该文对水包油乳液蛋白界面膜结构和影响因素进行探讨,系统综述了目前用于评价蛋白质界面特性的手段和方法,包括微观成像技术、热力学技术、光谱技术和界面流变学技术等,以研究蛋白类乳化液性能在宏观和微观层面的联系,为蛋白质界面膜在乳化食品中的应用提供参考。