Johnson P, Williams R R
Biochim Biophys Acta. 1983 Sep 14;747(1-2):1-9. doi: 10.1016/0167-4838(83)90113-9.
The C-terminal sequence of chicken gizzard desmin has been examined by computer programs based on Chou-Fasman prediction of secondary structure, auto-correlation and Fourier analysis of hydrophobic residue distribution, and cross-correlation analysis of acidic and basic residues. These analyses indicate that, although parts of the desmin sequence are alpha-helical, the helical regions may not be as extensive as predicted previously. Detailed analysis of the distribution of the charged residues in the desmin sequence strongly suggests that it cannot form a tropomyosin-like coiled-coil double-helix because of the almost complete absence of stabilizing salt-bridge interactions between proximal pairs of acidic and basic residues. Although the desmin sequence does contain the tropomyosin-like hydrophobic residue distribution, differences exist in the overall distributions of hydrophobes, with clusters of these residues being found in certain regions of the desmin sequence. Analyses of the sequences of porcine desmin and vimentin reveal very similar structural characteristics for these molecules, although vimentin is predicted to have a different structure at its C-terminus.
基于Chou-Fasman二级结构预测、疏水残基分布的自相关和傅里叶分析以及酸性和碱性残基的互相关分析的计算机程序，对鸡肌胃结蛋白的C末端序列进行了研究。这些分析表明，尽管结蛋白序列的部分区域是α螺旋，但螺旋区域可能不像之前预测的那么广泛。对结蛋白序列中带电残基分布的详细分析强烈表明，由于近端酸性和碱性残基对之间几乎完全缺乏稳定的盐桥相互作用，它无法形成原肌球蛋白样的卷曲螺旋双螺旋结构。尽管结蛋白序列确实包含原肌球蛋白样的疏水残基分布，但疏水基团的整体分布存在差异，在结蛋白序列的某些区域发现了这些残基的簇。对猪结蛋白和波形蛋白序列的分析揭示了这些分子非常相似的结构特征，尽管预测波形蛋白在其C末端具有不同的结构。
