Spermadhesin-1 Protein Analysis

Result and discussion

The sequence similarity of target sequence of buffalo spermadhesin-1 protein with other bovidiae sub family like caprinea and antilopinea was similarity in blastn search. They are shows the more than 65% sequence similarity. The physiochemical parameters of spermadhesin-1 protein were predicted by the help of Prot Param tool. The Prot Param describe the various parameters like molecular weight, theoretical PI, instability index (II), aliphatic index (AI), and grand average of hydropathicity (GRAVY).

The physiochemical properties of spermadhesin-1 molecule of Bubalis bubalis showed that the molecular weight of protein is 15339.6 contain 136 amino acid residues. It also contain the 21 number of leucine amino acid which have

Homology modeling

Homology modeling of the given protein sequence shows that the antipareller beta sheet are arranged in the spermadhesin-1 molecules .it shows that the protein molecule are stable nature. Motif Finding Figure 2- Motif predicted in spermadhesin-1 protein of bovidae family. The amino acid and position are shown on the x axis and height of the amino acid stacks shown on the y axis.

In the given set of spermadhesin-1 protein of bovidae family we found the three motifs. The first two motifs are having the protein of 50 amino acid sequences and the third motif have the protein of 29 amino acid sequences.

Table 1- Parameter computed using Prot Param

Alanine protein molecule is shows the aliphatic nature and belongs to non polar amino acid group. We found an increasing trend of ALA residues as we move from bovinae to antilopinae, reverse trend was found for ARG residue. In the bovinae family has the less residues in GLN and THR comparison to antilopinae family. Threonine belongs to polar uncharged amino acid group properties. GLU residue present in the more amount in the bovinae subfamily as compared to caprinae and antilopinae subfamily. Glutamine belongs to negative charged amino acid groups.

The α-helix is mostly found in the secondary structure of a protein sequence and it is most prevalent in protein structure. Methionin, Alanine, uncharged Leucine, Glutamate and Lysine mostly have the property to forming the alpha helix. Proline and Glycine have the poor helix forming properties Random coil shows the energetic stabilization of the protein molecule. It also useful for the calculation of energy barrier required for the folding of protein molecule.

Table 4- Amino Acid Property Group