PREDICTED SECONDARY STRUCTURE OF MALTODEXTRIN PHOSPHORYLASE FROM ESCHERICHIA-COLI AS DEDUCED USING CHOU-FASMAN MODEL

Secondary structure of maltodextrin Phosphorylase from Escherichia coli has been predicted using Chou-Fasman model. The enzyme protein contains 28% α-helix, 27% β-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 β-pleated sheets and two joining α-helix, are predicted. © 1990 Indian Academy of Sciences.