FT-Raman光谱研究金属硫蛋白的折叠过程  

INVESTIGATION ON THE FOLDING OF METALLOTHIONEIN BY FT-Raman SPECTROSCOPY

作　　者：高宏[1] 周群[1] 郁鉴源[1] 

机构地区：[1]清华大学化学系,北京100084

出　　处：《生物物理学报》1999年第3期445-450,共6页Acta Biophysica Sinica

摘　　要：为探索金属硫蛋白（ ＭＴ） 的折叠过程，寻找含硫蛋白折叠的动力，采用调节溶液ｐＨ 值的方法，使ＭＴ 处于不同的折叠状态。 测定了在ｐＨ１ ．０ － ７ ．５ 时溶液的Ｒａｍａｎ 谱， 进而得出ＭＴ 结构的变化。实验数据表明，在ｐＨ＝ ４ 时蛋白质的二级结构出现了两个转折点，提示ＭＴ 折叠过程中有两个中间态存在。根据实验结果，对ＭＴ 主链折叠的动力进行了讨论。In order to probe the folding process and motive force of Metallothionein(MT), the method of adjusting solution's pH was adopted to acquire MT at its various folding state. Investigating the Raman spectra of MT solution at pH between 1.0 and 7.5, the structure changes were obtained. The results indicated: at pH=3 and pH=4, there were two turning points in the content changing of MT's different secondary structures, showing two intermediate states in MT's folding process. The motive force of the main chain folding of MT was discussed.

关 键 词：蛋白质折叠 折叠动力 金属硫蛋白 拉曼光谱 

分 类 号：Q513.01[生物学—生物化学]