Lazović J
Laboratory for Multidisciplinary Research 180/2, Institute of Nuclear Sciences Vinća, Belgrade, Yugoslavia.
Comput Appl Biosci. 1996 Dec;12(6):553-62. doi: 10.1093/bioinformatics/12.6.553.
Fourier analysis of the parametric profile of a sequence for the detection and localization of the structural motifs that are characteristic for biologically related proteins has been proposed. In order to select parameters that are most appropriate for this analysis, the informational capacity of 226 physicochemical, thermodynamic, structural and statistical amino acid parameters was analyzed. Based on the results, obtained for the four functionally unrelated protein model groups (lysozyme c, HIV-1 gp120, tubulin and tau proteins, and steroid hormone receptors), the electron-ion interaction potential has been selected as the unique amino acid property that can be used in Fourier transform-based analysis of proteins, independently of their biological function.
有人提出对序列的参数轮廓进行傅里叶分析，以检测和定位与生物相关蛋白质特征性的结构基序。为了选择最适合该分析的参数，分析了226个物理化学、热力学、结构和统计氨基酸参数的信息容量。基于对四个功能不相关的蛋白质模型组（溶菌酶c、HIV-1 gp120、微管蛋白和tau蛋白以及类固醇激素受体）获得的结果，电子-离子相互作用势已被选为可用于基于傅里叶变换的蛋白质分析的独特氨基酸特性，而与它们的生物学功能无关。
