To investigate the surface accessisbility , antigenecity and hydrophobicity a protein sequence of 527 amino acids were taken from Dracunculus medinensis and in- depth study were conducted through various B-cell epitopes prediction methods, hydrophobicity prediction methods which provides the highest accurate outcomes. In course of the investigation we detected the maximal hydrophilicity region that could be an antigenic site, which also posses hydrophobic characteristics, because of well studied fact that an antigenic protein’s terminal region is likely unstructured and solvent accessible and moreover antibodies against this regions are likely to discern the native protein. We also predicted the antigenicity capacity of 527 amino acid sequence protein and found more antigenic and this protein segment can take active role in immunity of host and can effectively illustrate responses of immune of host. Along with other investigation of protein we also investigated protein’s Solvent accessibility, protein residues’ polarity to identify the regions which is exposed on the surface of proteins because it is essential point to focus because it can led to detect out the potential target active site and for development of the specific targeted drugs for cure.
