The contribution of two disulfide bonds in the trypsin binding domain of horsegram (Dolichos biflorus) Bowman-Birk inhibitor to thermal stability and functionality

The disulfide C20/C66 in the trypsin subdomain of horsegram (Dolichos biflorus) seed Bowman Birk inhibitor is pivotal for thermal and conformational stability. Long range interactions, between the two subdomains are facilitated by this disulfide.