Protein Structure and Function

The rate of hydrolysis of casein, ovalbumin, bovine serum albumin (BSA), arachin (from
groundnut, glycinin (from soybean), alpha_globulin (from sesame) and l1s protein from sunflower,
by trypsin or pepsin has been measured. The rates of hydrolysis have beeo correlated with intrinsic
viscosity and a-helical content of these proteins. The rates obtained by trypsin hydrolysis correlated
well with both intrinsic viscosity and alpha helical content of the proteins whereas the rates obtained with
pepsin correlated with intrinsic viscosity alone; the rates could not be correlated with alpha helical content.