| Literature DB >> 25952139 |
Jinyu Li1,2, Carlo Santambrogio3, Stefania Brocca3, Giulia Rossetti1,4, Paolo Carloni1, Rita Grandori3.
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.Entities:
Keywords: charge-state distributions; gas-phase basicity; molecular-dynamics simulations; proton transfer reactions; solvent accessible surface area
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Year: 2015 PMID： 25952139 DOI： 10.1002/mas.21465
Source DB: PubMed Journal: Mass Spectrom Rev ISSN： 0277-7037 Impact factor: 10.946