FEBS Letters | |
Bovine inositol monophosphatase: proteolysis and structural studies | |
Gore, M.G.1  Greasley, P.J.1  Ragan, C.I.2  Rees-Milton, K.J.1  | |
[1] Dept. of Biochemistry, Centre of Molecular Recognition, School of Biological Sciences, University of Southampton. Bassett Crescent East, Southampton, S09 3TU, UK;Neurosciences Research Centre, Merck Sharp and Dohme. Terlings Park, Eastwick Road, Harlow, Essex, CM20 2QR, UK | |
关键词: Inositol monophosphatase; Proteolysis; Protein structure; Circular dichroism; | |
DOI : 10.1016/0014-5793(93)80035-S | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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].
【 授权许可】
Unknown
【 预 览 】
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RO201912020297570ZK.pdf | 600KB | download |