Garcia-Quintana D, Garriga P, Manyosa J
Departament de Bioquímica i de Biologia Molecular, Facultat de Medicina, Universitat Autònoma de Barcelona, Spain.
Biochim Biophys Acta. 1992 Aug 21;1122(3):269-72. doi: 10.1016/0167-4838(92)90403-z.
Fourier transform-infrared spectroscopy has been used for the study of the secondary structure of arrestin from bovine retina rod cells. Spectra have been obtained in H2O and in D2O media. Resolution enhancement of the amide I secondary structure-sensitive overlapped component bands has been achieved by means of Fourier self-deconvolution and Fourier derivation. In order to obtain a quantitative estimation of the proportion of amino acid residues involved in each type of secondary structure, bands at the resolved frequencies have been curve-fitted to the deconvolved amide I contour by means of a least-squares best-fitting iterative program. The analysis of the results suggests that the secondary structure of arrestin comprises 56-63% of extended strands, 12-19% of turns and bends, 15% of alpha-helices and 10% of undefined and irregular segments.
傅里叶变换红外光谱已被用于研究牛视网膜视杆细胞中抑制蛋白的二级结构。已在H2O和D2O介质中获得光谱。通过傅里叶自去卷积和傅里叶微分实现了酰胺I二级结构敏感重叠成分带的分辨率增强。为了定量估计参与每种二级结构类型的氨基酸残基比例，已通过最小二乘最佳拟合迭代程序将分辨频率处的谱带与去卷积后的酰胺I轮廓进行曲线拟合。结果分析表明，抑制蛋白的二级结构包括56 - 63%的伸展链、12 - 19%的转角和弯曲、15%的α-螺旋以及10%的未定义和不规则片段。
