Predicted secondary structure of maltodextrin Phosphorylase from Escherichia coli as deduced using Chou-Fasman model.

ABSTRACT

Secondary structure of maltodextrin Phosphorylase from Escherichia coli has been predicted using Chou-Fasman model. The enzyme protein contains 28% α-helix, 27% ß-pleated sheets and 20% reverse β-turns. The secondary structure predicted 4 regions showing Rossman-fold super secondary structure. Two regions, one from residue 268–361 and the another from residue 606–684, having 4 consecutive strands of parallel β-pleated sheets and 3 joining α-helix, are predicted. Two regions, one from residue 379–434 and the another from residue 496–573, having 3 consecutive strands of parallel ß-pleated sheets and two joining α-helix, are predicted.