| Literature DB >> 27778278 |
Yu Qian1, Eranthie Weerapana2.
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.Entities:
Keywords: Chemically cleavable azobenzene linker; Cu + click; Cysteine-reactivity; Iodoacetamide-alkyne; MudPIT; isoTOP-ABPP
Mesh:
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Year: 2017 PMID: 27778278 PMCID: PMC5359601 DOI: 10.1007/978-1-4939-6439-0_2
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745