Emel'ianenko V I, Grishchenko V M, Burshteĭn E A
Biofizika. 2007 Sep-Oct;52(5):785-91.
Structural transitions in the tetrameric melittin from bee venom in 2 M KCl induced by variations of pH (from 0.7 to 12.0) and temperature (from 2 to 95 degrees C) have been studied. The pH and temperature ranges of structural changes and the zones of emission quenching of discerning tryptophan classes were revealed. The analysis of the temperature dependence of monotonic changes of spectral maximum positions and relative fluorescence yields allowed one to discriminate the zone of structural transitions in the tetramer from that of temperature quenching due to the thermal activation of fluorophore collisions with neighboring quenching groups in protein. Based on the new and earlier published results, some advantages and modes of using the method of component analysis of protein tryptophan spectra were summarized to determine the main characteristics of physicochemical transitions in proteins.
研究了在2M KCl中，pH值（从0.7到12.0）和温度（从2到95摄氏度）变化诱导的蜂毒四聚体蜂毒肽的结构转变。揭示了结构变化的pH值和温度范围以及区分不同色氨酸类别的发射猝灭区域。通过分析光谱最大位置和相对荧光产率单调变化的温度依赖性，能够区分四聚体中结构转变区域与由于荧光团与蛋白质中相邻猝灭基团热碰撞导致的温度猝灭区域。基于新的和早期发表的结果，总结了使用蛋白质色氨酸光谱成分分析方法来确定蛋白质物理化学转变主要特征的一些优点和模式。
