title: A pH-tunable peptide ligase.
abstract: A chemical ligation system is reported, in which a highly acidic coiled-coil peptide was used to template two basic peptide fragments and catalyze their condensation, in a pH-tunable fashion, to generate a coiled-coil product. This template showed a high catalytic efficiency (with single turnover) under neutral conditions. Under acidic conditions, however, its catalytic efficiency was reduced by approximately 4500-fold.
authors.affiliation: Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
authors.forename: S
authors.initials: S
authors.lastname: Yao
authors.forename: J
authors.initials: J
authors.lastname: Chmielewski
mesh_terms: D000595:Amino Acid Sequence; D019077:Helix-Turn-Helix Motifs; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008025:Ligases / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis*; D015202:Protein Engineering
chemical_list: D010446:Peptide Fragments; D008025:Ligases