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Abstract
We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on-demand for enabling ligation reactions down to peptide concentrations as low as a few hundreds nM at rates approaching 30 M-1 s-1.
Supplementary materials
Title
Fast protein modification in the nanomolar concentration range using an oxalyl amide as latent thioester_SI
Description
The Supporting Information details experimental procedures, data fitting and characterization for all organic compounds, peptides and proteins. The X-ray crystallographic coordinates for the structures reported in this study have been deposited at the Cambridge Crystallograph-ic Data Centre (CCDC) under deposition number CCDC 2164270. These data can be obtained free of charge from the Cambridge Crystallographic Data Centre via www.ccdc.cam.ac.uk/data_request/cif.
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