Gromiha M M, Majumdar R, Ponnuswamy P K
International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Protein Eng. 1997 May;10(5):497-500. doi: 10.1093/protein/10.5.497.
The membrane assembly of outer membrane proteins is more complex than that of transmembrane helical proteins owing to the intervention of many charged and polar residues in the membrane. Accordingly, the predictive accuracy of transmembrane beta strands is considerably lower than that of transmembrane alpha helices. In this paper we develop a set of conformational parameters for membrane spanning beta strands. We formulate an algorithm to predict the transmembrane beta strands in the family of bacterial porins based on the conformational parameters and surrounding hydrophobicities of amino acid residues. A Fortran program has been developed which takes the amino acid sequence as the input file and gives the predicted transmembrane beta strand as output. The present method predicts at an accuracy level of 82% for all the bacterial porins considered.
由于膜中存在许多带电和极性残基,外膜蛋白的膜组装比跨膜螺旋蛋白更为复杂。因此,跨膜β链的预测准确性远低于跨膜α螺旋。在本文中,我们开发了一组用于跨膜β链的构象参数。我们基于氨基酸残基的构象参数和周围疏水性,制定了一种算法来预测细菌孔蛋白家族中的跨膜β链。已经开发了一个Fortran程序,该程序将氨基酸序列作为输入文件,并将预测的跨膜β链作为输出。对于所有考虑的细菌孔蛋白,本方法的预测准确率为82%。