期刊
ANALYTICAL CHEMISTRY
卷 92, 期 9, 页码 6637-6644出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.0c00463
关键词
-
资金
- National Institutes of Health [R01 GM 075092, GM 128181]
- National Institutes of Health NIH [S10OD010645]
A new covalent labeling (CL) reagent based on an alpha,beta-unsaturated carbonyl scaffold has been developed for studying protein structure and protein-protein interactions when coupled with mass spectrometry. We show that this new reagent scaffold can react with up to 13 different types of residues on protein surfaces, thereby providing excellent structural resolution. To illustrate the value of this reagent scaffold, it is used to identify the residues involved in the protein-protein interface that is formed upon Zn(II) binding to the protein beta-2-microglobulin. The modular design of the alpha,beta-unsaturated carbonyl scaffold allows facile variation of the functional groups, enabling labeling kinetics and selectivity to be tuned. Moreover, by introducing isotopically enriched functional groups into the reagent structure, labeling sites can be more easily identified by MS and MS/MS. Overall, this reagent scaffold should be a valuable CL reagent for protein higher order structure characterization by MS.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据