In silico sequence analysis and prediction of 3-D structure of trypsin inhibitorin Zea mays by homology modelling

Present study deals with sequence analysis and homology modelling of maize trypsin inhibitor. The maize trypsin inhibitor was in the form of random coil (59.20%), extended strand (21.26%), alpha helix (14.37%) and abeta turn (5.17%). There were 5 antigenic determinants. The determinants 1 and 5 had peptide sequence SPVIPATMLVVALLVASSTVCFG (22) and GDGFVCRDWIFSLLEPPVCTPRPWDCCDFAVCTRDYIPYCQCGDVVESCP SNCKACKLVES (60) respectively, which were potentially antigenic. The hydropathy indices of all amino acids divided by the number of residues in the sequence, for protein molecule under study was-0.076, indicating the possibility of better interaction with water. In all five models were generated, out of them best model was selected on the basis of C-score (−3.26) for further process. The sequence analysis was performed with respect to secondary structure and antigenicity prediction. The 3D structure was predicted by using modeller and evaluated.