Bovine brain inositol monophosphatase is inactivated when trypsin catalyses the cleavage of a single peptide bond between Lys-36 and Ser-37. This proteolysis is closely followed by cleavage at two other sites in the protein between Lys-78 and Ser-79 and between Lys-156 and Ser-157 suggesting that all of these sites are exposed in the native conformation of the protein. All of these residues are predicted to lie at the ends of α helices. The most susceptible bond (Lys-36-Ser-37) is predicted to lie in a highly flexible region of the protein. Circular dichroism studies suggest that approximately 40% of the secondary structure of this protein is helical which is similar to that predicted by the algorithm of Gamier et al. [(1978) J. Mol. Biol. 120, 97-120]. © 1993.
Greasley, P. J., Gore, M. G., Rees-Milton, K. J., & Ragan, C. I. (1993). Bovine inositol monophosphatase: proteolysis and structural studies. FEBS Letters, 319(1–2), 49–53. https://doi.org/10.1016/0014-5793(93)80035-S