Identification of membrane spanning beta strands in bacterial porins

被引:57
作者
Gromiha, MM
Majumdar, R
Ponnuswamy, PK
机构
[1] UNIV MADRAS,MADRAS 600005,TAMIL NADU,INDIA
[2] INT CTR GENET ENGN & BIOTECHNOL,I-34012 TRIESTE,ITALY
[3] SAHA INST NUCL PHYS,DIV BIOPHYS,CALCUTTA 700037,W BENGAL,INDIA
来源
PROTEIN ENGINEERING | 1997年 / 10卷 / 05期
关键词
bacterial porin; conformational parameter; prediction; surrounding hydrophobicity; transmembrane beta strands;
D O I
10.1093/protein/10.5.497
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:497 / 500
页数:4
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