Characterization And Structural Annotation Of Renin And Angiotensin Converting Enzymes.

The physicochemical properties of amino acids, peptides and proteins depends on the presence of side chain,. hydrophobic groups, neutral and hydrophilic groups. This property influences the secondaryand tertiary structures and functions of proteins .So this study was proposed to characterize Renin and Angiotensin converting enzymes, using expasy proteomics tools. The Theoretical pI of all enzymes are above 5, all enzymes had more number of negatively charged residues than positively charged residues. Extinction coefficient of all enzymes are above 1, plasma half life is more than 30 hrs and aliphatic index is more than 75, instability index is greater than 40 , Grand average of hydropathicity is above 0.37 for all 3 ACE’s and for renin it is 0.114. The 3 ACE’s has more number of amino acids forming alpha helix than beta sheets. For renin beta sheet is more than alpha helix. Remaining structure is occupied by random coil.