期刊
MASS SPECTROMETRY REVIEWS
卷 35, 期 1, 页码 111-122出版社
WILEY
DOI: 10.1002/mas.21465
关键词
charge-state distributions; proton transfer reactions; solvent accessible surface area; molecular-dynamics simulations; gas-phase basicity
类别
资金
- John von Neumann Institute for Computing (NIC), Germany
Electrospray-ionization mass spectrometry (ESI-MS) is a key tool of structural biology, complementing the information delivered by conventional biochemical and biophysical methods. Yet, the mechanism behind the conformational effects in protein ESI-MS is an object of debate. Two parameterssolvent-accessible surface area (A(s)) and apparent gas-phase basicity (GB(app))are thought to play a role in controlling the extent of protein ionization during ESI-MS experiments. This review focuses on recent experimental and theoretical investigations concerning the influence of these parameters on ESI-MS results and the structural information that can be derived. The available evidence supports a unified model for the ionization mechanism of folded and unfolded proteins. These data indicate that charge-state distribution (CSD) analysis can provide valuable structural information on normally folded, as well as disordered structures. (c) 2015 Wiley Periodicals, Inc.
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