Raman Characterizing Disulfide Bonds and Secondary Structure of Bovine Serum Albumin

摘要

Bovine Serum Albumin (BSA) is a globular protein of molecular mass –66 kDa. It consists of 580 amino acids residues with 17 intrachain disulfide bonds with one free thiol group at residue 34 [1, 2]. The secondary structure of BSA was reported approximately 54% in a-helix and 40% in b-form b-sheet plus (3-turn). The conformation of BSA is susceptible to physically and chemically denaturing treatments. The secondary structure tends to rearrange from a-helical to 13-form under thermal denaturation [3]. How conformational change correlates to high content of disulfide bonds of BSA draws much interest. In this report, FT-Raman was employed to elucidate the effect of disulfide bonds on the secondary structure of BSA and in turn to clarify the effect of disulfide bonds on the stability of protein.