Identification of membrane spanning beta strands in bacterial porins.
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.
Gromiha
M M
MM
International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Majumdar
R
R
Ponnuswamy
P K
PK
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000737:chemistry; D004926:Escherichia coli; D008969:Molecular Sequence Data; D018272:Porins / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016992:Rhodobacter; D016354:Rhodobacter capsulatus
D018272:Porins