Ontology highlight
ABSTRACT:
SUBMITTER: O'Donoghue AJ
PROVIDER: S-EPMC3707110 | biostudies-other | 2012 Nov
REPOSITORIES: biostudies-other
O'Donoghue Anthony J AJ Eroy-Reveles A Alegra AA Knudsen Giselle M GM Ingram Jessica J Zhou Min M Statnekov Jacob B JB Greninger Alexander L AL Hostetter Daniel R DR Qu Gang G Maltby David A DA Anderson Marc O MO Derisi Joseph L JL McKerrow James H JH Burlingame Alma L AL Craik Charles S CS
Nature methods 20120930 11
We developed a simple and rapid multiplex substrate-profiling method to reveal the substrate specificity of any endo- or exopeptidase using liquid chromatography-tandem mass spectrometry sequencing. We generated a physicochemically diverse library of peptides by incorporating all combinations of neighbor and near-neighbor amino acid pairs into decapeptide sequences that are flanked by unique dipeptides at each terminus. Addition of a panel of evolutionarily diverse peptidases to a mixture of the ...[more]