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

• 来源期刊: 中国科学B辑（英文版）
• 年，卷（期）: 2009,（6）
• 页码范围: 809-814
• 页数: 6页
• 语种: 英文
• DOI: 10.1007/s11426-009-0027-x

摘要

The polarity-sensitive fluorescent probe, 3-(4-chloro-6-p-glyoxalphenoxy-1,3,5-triazinylamino)-7-(dimethyl-amino)-2-methylphenazine, was used to analyze the local structure of apo-a-lactalbumin by detecting the polarity and conformational changes of the arginine residue (Arg10) domain. The polarity of the Arg10 do-main in both native and heat-denatured apo-a-lactalbumln was determined, which corresponds to a dielectric constant of 16, and the hydrophobic core near the Arg10 was found to be conservative for heating. Mean-while, 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+.