title: A Quantitative Mass-Spectrometry Platform to Monitor Changes in Cysteine Reactivity.
abstract: Cysteine residues on proteins serve diverse functional roles in catalysis and regulation and are susceptible to numerous posttranslational modifications. Methods to monitor the reactivity of cysteines within the context of a complex proteome have facilitated the identification and functional characterization of cysteine residues on disparate proteins. Here, we describe the use of a cysteine-reactive iodoacetamide probe coupled to isotopically labeled, cleavable linkers to identify and quantify cysteine-reactivity changes from two biological samples.
authors: Department of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, MA, USA.
authors: Yu
authors: Y
authors: Qian
authors: Department of Chemistry, Boston College, 2609 Beacon Street, Chestnut Hill, MA, USA. eranthie@bc.edu.
authors: Eranthie
authors: E
authors: Weerapana
mesh_terms: D000818:Animals; D003545:Cysteine / Q000737:chemistry*; D007460:Iodoacetamide / Q000737:chemistry; D013058:Mass Spectrometry / Q000379:methods*; D011499:Protein Processing, Post-Translational; D020543:Proteome
chemical_list: D020543:Proteome; D003545:Cysteine; D007460:Iodoacetamide
keywords: Chemically cleavable azobenzene linker; Cu + click; Cysteine-reactivity; Iodoacetamide-alkyne; MudPIT; isoTOP-ABPP