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Resonance Assignments of Lowly Populated and Unstable Enzyme Intermediate Complex under Real‐Time Conditions
Author(s) -
Chen JiaLiang,
Wang Xiao,
Xiao YuHao,
Su XunCheng
Publication year - 2019
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201900240
Subject(s) - resonance (particle physics) , enzyme , chemistry , physics , biophysics , chemical physics , biochemistry , atomic physics , biology
Abstract Unstable and low‐abundance protein complexes represent a large family of transient protein complexes that are difficult to characterize, even by means of high‐resolution NMR spectroscopy. A method to assign the NMR signals of these unstable complexes through a combination of selective isotope labeling of amino acids in a protein and site‐specific labeling the protein with a paramagnetic tag is presented herein. By using this method, the resonances of unstable thioester intermediate complex (lifetime <5 h and highest concentration ≈20 μ m ) generated by Staphylococcus aureus sortase A and its peptide substrate under a real‐time reaction have been assigned.

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