期刊
INTERNATIONAL JOURNAL OF MASS SPECTROMETRY
卷 300, 期 2-3, 页码 118-122出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijms.2010.06.032
关键词
Electrospray ionization; Noncovalent complex; Supercharging; Protein-ligand binding; Adenylate kinase; Carbonic anhydrase
资金
- National Institutes of Health [RR 20004]
- NIH/NCRR [S10 RR023045]
Tandem mass spectrometry (MS/MS) of intact, noncovalently bound protein-ligand complexes can yield structural information on the site of ligand binding. Fourier transform ion cyclotron resonance (FT-ICR) top-down MS of the 29 kDa carbonic anhydrase-zinc complex and adenylate kinase bound to adenosine triphosphate (ATP) with collisionally activated dissociation (CAD) and/or electron capture dissociation (ECD) generates product ions that retain the ligand and their identities are consistent with the solution phase structure. Increasing gas phase protein charging from electrospray ionization (ESI) by the addition of supercharging reagents, such as m-nitrobenzyl alcohol and sulfolane, to the protein analyte solution improves the capability of MS/MS to generate holo-product ions. Top-down proteomics for protein sequencing can be enhanced by increasing analyte charging. (C) 2010 Elsevier B.V. All rights reserved.
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