Thermodynamics of protein folding: methodology, data analysis and interpretation of data

被引:17
作者
Shirdel, Seyedeh Akram [1 ]
Khalifeh, Khosrow [2 ]
机构
[1] Tarbiat Modares Univ, Fac Biol Sci, Dept Biochem, Tehran, Iran
[2] Univ Zanjan, Fac Sci, Dept Biol, Univ Blvd, Zanjan 4537138791, Iran
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2019年 / 48卷 / 04期
关键词
Thermodynamics; Folding; Stability; Equilibrium; Protein; Data analysis; GUANIDINE-HYDROCHLORIDE DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; MOLAR HEAT-CAPACITY; COLD DENATURATION; CONFORMATIONAL STABILITY; THERMAL-DENATURATION; ALPHA-CHYMOTRYPSIN; AGGREGATION; MICROCALORIMETRY; DEHYDROGENASE;
D O I
10.1007/s00249-019-01362-7
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Thermodynamics of protein folding refers to the stability measurements where structural changes of a given protein in the presence of a denaturing agent are monitored by spectroscopic or calorimetric techniques. In macroscopic point of view, protein stability represents the ratio of the population of its unfolded state to that of folded one in equilibrium condition, while in microscopic point of view, the stability is actually a net value from a combination of favorable and unfavorable contributions that affect the structural integrity of a protein molecule. In this manuscript, the principles and methodological aspects of thermodynamic studies and methods of data analysis as well as interpretation of the results are presented. [GRAPHICS] .
引用
收藏
页码:305 / 316
页数:12
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