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| Home > Publications database > Conformational effects in protein electrospray-ionization mass spectrometry |
| Journal Article | FZJ-2016-00240 |
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2016
Wiley
New York, NY [u.a.]
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Please use a persistent id in citations: doi:10.1002/mas.21465
Abstract: 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 parameters—solvent-accessible surface area (As) and apparent gas-phase basicity (GBapp)—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.
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