QQ客服 官方微博 反馈留言

	Calorimetric determination of enthalpies of lysozyme folding at a liquid-solid interface
	Geng, XP ; Zhang, HF ; Wang, BH ; Geng, XD ; Xing, JW
	2005
关键词	liquid-solid interface lysozyme micro-calorimetry protein folding HYDROPHOBIC INTERACTION CHROMATOGRAPHY RETENTION MECHANISM PROTEINS
英文摘要	Calorimetric determination of the total enthalpy changes (Delta H-i) of guanidine-denatured lysozyme (Lys) during the adsorption with simultaneously refolding on the surface of hydrophobic interaction chromatography packings was carried out at 25 +/- 0.001 degrees C. The measured Delta H-i in the circumstances should include the changes in the three fractions: adsorption, dehydration and molecular conformation. It was found that when the unfolded Lys molecules are adsorbed and refold on the surface, entropy-driving caused by the dehydration of Lys mainly dominates the foregoing process. The refolding enthalpies of Lys, Delta Delta H-i were found to be 10 similar to 100 folds higher than that measured in usual solutions.; Chemistry, Analytical; Chemistry, Physical; SCI(E); CPCI-S(ISTP); 10
语种	英语
DOI标识	10.1007/s10973-005-6926-y
内容类型	其他
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/254196]
专题	化学与分子工程学院
推荐引用方式 GB/T 7714	Geng, XP,Zhang, HF,Wang, BH,et al. Calorimetric determination of enthalpies of lysozyme folding at a liquid-solid interface. 2005-01-01.

个性服务

查看访问统计

相关权益政策

暂无数据

收藏/分享

除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。