肌红蛋白
变性(裂变材料)
热力学
工作(物理)
蛋白质动力学
动力学(音乐)
分子动力学
大气温度范围
化学物理
材料科学
热的
蛋白质折叠
化学
物理
计算化学
生物化学
声学
核化学
作者
Ramzi R. Khuri,Trung Phan,Robert H. Austin
出处
期刊:Physical review
日期:2021-09-24
卷期号:104 (3)
标识
DOI:10.1103/physreve.104.034414
摘要
We reinvestigate a simple model used in the literature concerning the thermodynamic analysis of protein cold denaturation. We derive an exact thermodynamic expression for cold denaturation and give a better approximation than exists in the literature for predicting cold denaturation temperatures in the two-state model. We discuss the "dark-side" implications of this work for previous temperature-dependent protein dynamics experiments and discuss microfluidic experimental technologies, which could explore the thermal stability range of proteins below the bulk freezing point of water.
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