A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods
A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods
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DOI：
10.1021/bi030149y
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发表时间：
2004-03-09
期刊：
影响因子：
2.9
通讯作者：
Singh, BR
中科院分区：
文献类型：
--
作者：
Cai, SW;Singh, BR
傅里叶变换红外光谱正成为研究蛋白质二级结构越来越重要的方法。蛋白质红外光谱的酰胺 I 区域是广泛使用的区域，而酰胺 III 区域由于其信号较低而相对被忽视。由于酰胺III区域没有水的干扰，更重要的是，不同的蛋白质二级结构在其酰胺III光谱中具有更清晰的差异，因此利用酰胺III区域来确定蛋白质二级结构是非常有前途的。在我们当前的研究中，使用偏最小二乘（PLS）方法从蛋白质红外光谱预测蛋白质二级结构。记录了16种已知晶体结构的不同蛋白质水溶液的红外光谱，并使用这些蛋白质的酰胺I、阳极III以及酰胺I与酰胺III区域的组合来建立PLS算法的校准集。我们的结果与 X 射线研究的数据非常相关，并且酰胺 III 区域的预测优于酰胺 I 或酰胺 I 和酰胺 III 区域的预测。
Fourier transform infrared spectroscopy is becoming an increasingly important method to study protein secondary structure. The amide I region of the protein infrared spectrum is the widely used region, whereas the amide III region has been comparatively neglected due to its low signal. Since there is no water interference in the amide III region and, more importantly, the different secondary structures of proteins have more resolved differences in their amide III spectra, it is quite promising to use the amide III region to determine protein secondary structure. In our current study, a partial least squares (PLS) method was used to predict protein secondary structures from the protein IR spectra. The IR spectra of aqueous solutions of 16 different proteins of known crystal structure have been recorded, and the amide I, the anode III, and the amide I combined with the amide III region of these proteins were used to set up the calibration set for the PLS algorithm. Our results correlate quite well with the data from X-ray studies, and the prediction from the amide III region is better than that from amide I or combined amide I and amide III regions.