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利用极性敏感的荧光探针3-(4-氯-6-p-甲酰甲醛基苯氧基-1,3,5-三嗪氨基)-7-二甲胺基-2-甲基吩嗪,开展了apo-α-乳白蛋白的区域结构研究,分析了该蛋白中Arg10区域的局部极性和构象变化;定量测定了天然的、热变性的apo-α-乳白蛋白的Arg10区域的介电常数,均为16.由此揭示出Arg10附近的疏水核对热变性是相对保守的.此外,还研究了Ca2+结合对Arg10的局部构象影响,结果表明,Ca2+的结合几乎不改变该区域的构象,提示Arg10附近的疏水核对Ca2+的结合也不敏感.
Using polar sensitive fluorescent probe 3- (4-chloro-6-p-formylformalphenoxy-1,3,5-triazinylamino) -7-dimethylamino- Oxazine, the regional structure of apo-a-lactalbumin was investigated and the local polarities and conformational changes of the Arg10 region in the protein were analyzed. The Arg10 region of natural, heat-denatured apo-a-lactalbumin The electrical constants are both 16. It was thus revealed that the hydrophobic nuclei near Arg10 are relatively conservative in thermal denaturation.In addition, the local conformational effects of Ca2 + binding on Arg10 were also studied and showed that the binding of Ca2 + hardly changed the conformation of this region , Suggesting that hydrophobic nuclei near Arg10 are also not sensitive to Ca2 + binding.