Shubin V V, Khazin M L, Efimovskaia T V
Mol Biol (Mosk). 1990 Jan-Feb;24(1):189-201.
A ridge regression method is presented for prediction of the secondary structure of proteins by the circular dichroism spectra (CD) from 190 to 236 nm. Eight types of the secondary structure were calculated on a microcalculator. The method is based on the X-ray data of Kabsh and Sander. The teaching rule is constructed on CD spectra of 30 proteins of all structural classes of the globular proteins (alpha, alpha/beta, alpha + beta and beta-proteins). The errors of the methods are analysed by removing each protein from the reference set and analyzing its structure in terms of the remaining proteins. Correlation coefficients and root-mean square deviations between CD and X-ray data were: 0.99 and 0.03 for alpha-helix, 0.86 and 0.02 for 3(10)-helix, 0.92 and 0.06 for antiparallel beta-sheet, 0.86 and 0.03 for parallel beta-sheet, 0.94 and 0.01 for T3 beta-turn, 0.85 and 0.02 for other beta-turn, 0.84 and 0.03 for S-bends, 0.83 and 0.04 for "random" structure.
提出了一种岭回归方法，用于根据190至236纳米的圆二色光谱（CD）预测蛋白质的二级结构。在微型计算器上计算了八种二级结构类型。该方法基于卡布希和桑德的X射线数据。教学规则是根据球状蛋白质所有结构类别的30种蛋白质的CD光谱构建的（α、α/β、α + β和β - 蛋白质）。通过从参考集中移除每种蛋白质并根据其余蛋白质分析其结构来分析该方法的误差。CD和X射线数据之间的相关系数和均方根偏差分别为：α - 螺旋为0.99和0.03，3(10)-螺旋为0.86和0.02，反平行β - 折叠为0.92和0.06，平行β - 折叠为0.86和0.03，T3β - 转角为0.94和0.01，其他β - 转角为0.85和0.02，S - 弯为0.84和0.03，“无规”结构为0.83和0.04。
