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首页> 外文期刊>Romanian Journal of Biophysics >EPR AND ATR-FT-IR INVESTIGATION OF LYOPHILIZED CYTOCHROME C AT DIFFERENT PH
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EPR AND ATR-FT-IR INVESTIGATION OF LYOPHILIZED CYTOCHROME C AT DIFFERENT PH

机译：不同pH下的冻融细胞色素C的EPR和ATR-FT-IR研究

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Conformational changes and interaction of spin label with cytochrome c protein at different pH value have been studied by FT-IR and EPR spectroscopy. Electron Paramagnetic Resonance (EPR) spectroscopy was used to investigate the mobility of Tempo spin label (3-carbamoyl-2,2,5,5-tetramethyl-3-pyrrolin-1-yloxy) in order to obtain useful information related to the interaction between the nitroxide group and the functional site of the lyophilized protein samples. A minimum mobility can be observed around the isoelectric point (pHi = 9.8). The best information from infrared protein spectra is obtained in the amide I band which appears between 1700 and 1600 cm–1. The results of qualitative and quantitative analysis by curve fitting to the inverted second derivative spectra of amide I features of lyophilized hemoglobin reveal a decrease in β-sheet content as the pH values increases and a decrease in α-helix content at lower or higher pH values as well as a decrease in turns content
机译：通过FT-IR和EPR光谱研究了不同pH值下自旋标记与细胞色素c蛋白的构象变化和相互作用。为了获得与相互作用有关的有用信息，使用电子顺磁共振（EPR）光谱研究了Tempo自旋标记（3-氨基甲酰基-2,2,5,5-四甲基-3-吡咯啉-1-基氧基）的迁移率。在硝酸根基团和冻干蛋白质样品的功能位点之间。可以在等电点（pHi = 9.8）附近观察到最小迁移率。在1700至1600 cm-1之间出现的酰胺I谱带中，可获得红外蛋白光谱的最佳信息。通过对冻干血红蛋白的酰胺I特征的反二阶导数光谱进行曲线拟合进行定性和定量分析的结果表明，随着pH值的增加，β-sheet含量降低，而在较低或较高的pH值时，α-螺旋含量降低以及转弯内容的减少

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