Analysis of local structure of Arg10 domain in apo-α- lactalbumin with a polarity-sensitive arginine-specific fluorescent probe

作     者：WANG ShuJuan CHEN SuMing MA HuiMin 

作者机构：Beijing National Laboratory for Molecular SciencesInstitute of ChemistryChinese Academy of SciencesBeijing 100190China 

出 版 物：《Science China Chemistry》 (中国科学（化学英文版）)

年 卷 期：2009年第52卷第6期

页      面：809-814页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070302[理学-分析化学] 0703[理学-化学] 

基　　金：Supported by the National Natural Science Foundation of China (Grant Nos. 20525517, 90813032 & 20875092) the 863 Program (Grant No. 2008AA02Z206) the Chinese Academy of Sciences 

主　　题：arginine-specific labeling fluorescent probes local polarity detection conformational changes Ca2+ binding 

摘      要：The polarity-sensitive fluorescent probe, 3-(4-chloro-6-p-glyoxalphenoxy-1,3,5-triazinylamino)-7- (dimethylamino)-2-methylphenazine, was used to analyze the local structure of apo-α-lactalbumin by detecting the polarity and conformational changes of the arginine residue (Arg10) domain. The polarity of the Arg10 domain in both native and heat-denatured apo-α-lactalbumin was determined, which corresponds to a dielectric constant of 16, and the hydrophobic core near the Arg10 was found to be conservative for heating. Meanwhile, the effect of Ca2+ binding on the conformational changes of the Arg10 domain was studied, revealing that the hydrophobic core near the Arg10 is insensitive to the binding of Ca2+.