Pollen allergies (Hey-fever) are the most common and wide spread and released from the plants for the purpose of fertilization and can be carried for miles by the wind. Unfortunately when there is too much pollen in the air, it causes problems to the sensitive persons, causing some ailments and allergic disorders. Therefore, it is prime need to characterize the allergic pollen proteins. In the present investigations, pollen-specific protein Bnm1 from Arabidopsis thaliana was screened in-silico for its allergic and antigenic characters. Pollen-specific protein Bnm1 having 187 amino acids residues, which shows five antigenic determinants. Motif map shows more receptors on B-cell than on T-cell. MHC-class 1 receptors are also found in motif map. Protein statistics is also carried out with respect to several parameters with the help of Peptool 2.0. Predicted results are support to elicit, the pollen-specific protein Bnm1 is allergic.

The pollen antigens are variable and the study of the antigenic/allergenic fractions of the allergens is of paramount importance. The recent findings and techniques from the fields of molecular biology, nanotechnology, bioinformatics and information technology (IT) has given further stimulation for the identification, characterization and comprehensive classification of the allergenic modules and their sources. Therefore, during the present investigations SRK protein from Brassica oleracea was screened in-silico for its allergic and antigenic characters. SRK protein contains 658 amino acids and has 25 antigenic determinants. Out of which 4-SYTFSFLLVFLVLILFHPALSIYVNT-29 and 567-QHNNLVRLLGCCVYEGEKILIYEYLD NLSLDSHLFD-602 fragment shows highest antigenicity. It shows 1.0273 averages antigenic propensity containing 50.7599% hydrophilic amino acids and 49.0881% hydrophobic amino acids. The SRK protein contains 72 basic amino acids and 69 acidic amino acids. The total linear charge density of the protein is 0.217325. The solubility of protein is 1.48797. The structural characters of the SRK protein show alpha-helix 29.9%, beta-sheet 28.3% and coil 41.8%. Motif map of SRK protein shows 509 motifs out of which 220 are MHC class I related, 200 motifs have functional relationship with B-cell membrane and others have functional relationship with T-cell membrane. Predicted results are sufficient to elicit the allergenicity of SRK protein.