Protein surface charge of trypsinogen changes its activation pattern

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Protein surface charge of trypsinogen changes its activation pattern

BACKGROUND Trypsinogen is the inactive precursor of trypsin, a serine protease that cleaves proteins and peptides after arginine and lysine residues. In this study, human trypsinogen was used as a model protein to study the influence of electrostatic forces on protein-protein interactions. Trypsinogen is active only after its eight-amino-acid-long activation peptide has been cleaved off by anot...

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The activation peptide of mammalian trypsinogens contains a highly conserved tetra-aspartate sequence (D19-D20-D21-D22) preceding the K23-I24 scissile peptide bond, which is hydrolyzed as the first step in the activation process. Here, we examined the evolution and function of trypsinogen activation peptides through integrating functional characterization of disease-associated mutations with co...

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Studies on the autocatalytic activation of trypsinogen.

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ژورنال

عنوان ژورنال: BMC Biotechnology

سال: 2014

ISSN: 1472-6750

DOI: 10.1186/s12896-014-0109-5