Fig. 6

Features of the secondary structure of AsAPN-1 (a) Hopp and Woods (1981) hydrophobicity plot of AsAPN-1. A negative value is associated with the non-polar residues and hydrophobic regions and values greater than 0 represent the hydrophilic regions. All residues which are located in the N-terminal and C-terminal of the AsAPN-1 have suitable hydrophilicity. b Accessibility of AsAPN-1 analysis using the Protscale-ExPASy server revealed that the most of residues which are located in the N-terminal and C-terminal of AsAPN-1 are accessible in the secondary structure and have a good position for presentation to immune system. In this prediction, values greater than 0 have suitable accessibility for immune system. c Amino acid polarity was determined by Protscale-ExPASy. Our results showed that the 230 and 200 residues of the N-terminal and C-terminal of AsAPN-1 are polar, respectively. dN-glycosylation; this analysis was performed by NetNglyc 1.0 server. Our analysis revealed that V2, N148, and N589 positions have acceptable score for N-glycosylation. e Prediction of dynamic nature of AsAPN1 using DynaMine server: Our results showed that the most of regions of AsAPN-1 are rigid, and there are only four flexible regions with the lowest predicted S2 value which are M1(0.59)-V2(0.61), G763-(0.62), Y764(0.62) and A975 (0.61)-G976(0.61) residues. In addition, there are two more flexible residues with the lowest S2 value which are L1024 (0.56)-G1025(0.50)