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首页> 外文期刊>The FEBS journal >Structural study of the catalytic domain of PKC zeta using infrared spectroscopy and two-dimensional infrared correlation spectroscopy
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Structural study of the catalytic domain of PKC zeta using infrared spectroscopy and two-dimensional infrared correlation spectroscopy

机译：红外光谱和二维红外相关光谱研究PKC zeta催化区域的结构

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The secondary structure of the catalytic domain from protein kinase C zeta was studied using IR spectroscopy. In the presence of the substrate MgATP, there was a significant change in the secondary structure. After heating to 80 degrees C, a 14% decrease in the alpha-helix component was observed, accompanied by a 6% decrease in the beta-pleated sheet; no change was observed in the large loops or in 3(10)-helix plus associated loops. The maximum increase with heating was observed in the aggregated beta-sheet component, with an increase of 14%. In the presence of MgATP, and compared with the sample heated in its absence, there was a substantial decrease in the 3(10)-helix plus associated loops and an increase in alpha-helix. Synchronous 2D-IR correlation showed that the main changes occurred at 1617 cm(-1), which was assigned to changes in the intermolecular aggregated beta-sheet of the denaturated protein. This increase was mainly correlated with the change in alpha-helix. In the presence of MgATP, the main correlation was between aggregated beta-sheet and the large loops component. The asynchronous 2D-correlation spectrum indicated that a number of components are transformed in intermolecularly aggregated beta-sheet, especially the alpha-helix and beta-sheet components. It is interesting that changes in 3(10)-helix plus associated loops and in alpha-helix preceded changes in large loops, which suggests that the open loops structure exists as an intermediate state during denaturation. In summary, IR spectroscopy revealed an important effect of MgATP on the secondary structure and on the thermal unfolding process when this was induced, whereas 2D-IR correlation spectroscopy allowed us to show the establishment of the denaturation pathway of this protein.
机译：使用红外光谱研究了蛋白激酶C zeta催化结构域的二级结构。在底物MgATP存在下，二级结构发生了显着变化。加热到80摄氏度后，观察到α-螺旋成分减少了14％，β-折叠片减少了6％;在大回路或3（10）-螺旋加相关回路中未观察到变化。在聚集的β-折叠组分中观察到随着加热的最大增加，增加了14％。在存在MgATP的情况下，与在不存在MgATP的情况下加热的样品相比，3（10）-螺旋加上相关的环显着减少，而α-螺旋则增加。同步2D-IR相关性显示主要变化发生在1617 cm（-1），该变化被指定为变性蛋白质的分子间聚集β-折叠的变化。这种增加主要与α-螺旋的变化有关。在存在MgATP的情况下，主要的相关性在于聚集的β-折叠和大环成分之间。异步2D相关光谱表明，许多组分在分子间聚集的β-折叠中发生了转化，尤其是α-螺旋和β-折叠中的组分。有趣的是，3（10）-螺旋加上相关联的环的变化以及在大环中的α-螺旋的变化先于大环的变化，这表明开环结构在变性过程中以中间状态存在。总之，IR光谱揭示了MgATP在诱导时对二级结构和热展开过程的重要作用，而2D-IR相关光谱则使我们能够显示该蛋白质的变性途径的建立。

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