Profiling Protein S‐Sulfination with Maleimide‐Linked Probes

Cysteine residues are susceptible to oxidation to form S‐sulfinyl (R‐SO2H) and S‐sulfonyl (R‐SO3H) post‐translational modifications. Here we present a simple bioconjugation strategy to label S‐sulfinated proteins by using reporter‐linked maleimides. After alkylation of free thiols with iodoacetamide...

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Bibliographic Details
Published in:	Chembiochem : a European journal of chemical biology Vol. 18; no. 20; pp. 2028 - 2032
Main Authors:	Kuo, Yu‐Hsuan, Konopko, Aaron M., Borotto, Nicholas B., Majmudar, Jaimeen D., Haynes, Sarah E., Martin, Brent R.
Format:	Journal Article
Language:	English
Published:	Germany Wiley Subscription Services, Inc 18-10-2017
Subjects:	Alkylation Cysteine Electron transport Electron transport chain Endoplasmic reticulum HEK293 Cells Humans Lipopolysaccharides Maleimides - chemistry Michael addition Models, Molecular Molecular Probes - chemistry Oxidation Pharmacology Post-translation Protein Conformation protein modifications Protein S Proteins Proteins - chemistry Proteins - metabolism redox chemistry Rodents Sulfinic Acids - metabolism sulfur Sulfur - metabolism Thiols Michael addition sulfur protein modifications cysteine redox chemistry
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