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运用ＦＴ－ＩＲ方法的分辨率增强及曲线拟合技术对水化膜中蚯蚓钙调素ＣａＭ的二级结构以及加入不同比例Ｃａ２＋、Ｔｂ３＋后ＣａＭ二级结构的变化进行了研究。结果表明，水化膜中ＣａＭ及含不同比例Ｃａ２＋或Ｔｂ３＋的蛋白复合物的α－ｈｅｌｉｘ的含量较晶体和溶液中为低，而β－ｓｈｅｅｔ和ｔｕｒｎ结构的含量相对较高。研究发现不同比例金属离子的加入，引起了ＣａＭ二级结构不同程度的变化，但各类结构在总量上观察不到明显的变化规律，且由于结合机制的不同，Ｃａ２＋和Ｔｂ３＋的影响也各不相同。Ｔｂ３＋可与ＣａＭ中的Ｃａ结合位点结合，在一定条件下激活ＣａＭ，但在较高浓度下，Ｔｂ３＋的结合抑制ＣａＭ的活性。
The secondary structure of earthworm calmodulin CaM in hydrated membrane and the change of secondary structure of CaM after Ca2 + and Tb3 + addition were studied by using the resolution enhancement and curve fitting of FT-IR method. The results showed that the α-helix content of CaM and protein complexes containing different proportions of Ca2 + or Tb3 + was lower than that of the crystal and solution, while the contents of β-sheet and turn structures were relatively high. The results showed that the addition of different proportions of metal ions caused different degrees of CaM secondary structure changes, but no obvious changes in the total structure of the various types of observed changes, and because of the different binding mechanisms, Ca2 + and Tb3 + Are not the same. Tb3 + binds to the Ca binding site in CaM, activating CaM under certain conditions, but binding of Tb3 + inhibits CaM activity at higher concentrations.