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A pH‐tunable peptide ligase
Author(s) -
Yao Shao,
Chmielewski Jean
Publication year - 1999
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1999)51:5<370::aid-bip7>3.0.co;2-t
Subject(s) - chemistry , peptide , catalysis , coiled coil , ligation , chemical ligation , condensation , dna ligase , combinatorial chemistry , electromagnetic coil , biochemistry , enzyme , thermodynamics , microbiology and biotechnology , electrical engineering , engineering , physics , biology
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. © 2000 John Wiley & Sons, Inc. Biopoly 51: 370–375, 1999