This title appears in the Scientific Report :
2016
Please use the identifier:
http://dx.doi.org/10.1002/mas.21465 in citations.
Conformational effects in protein electrospray-ionization mass spectrometry
Conformational effects in protein electrospray-ionization mass spectrometry
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-a...
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Personal Name(s): | Li, Jinyu |
---|---|
Santambrogio, Carlo / Brocca, Stefania / Rossetti, Giulia / Carloni, Paolo / Grandori, Rita (Corresponding author) | |
Contributing Institute: |
GRS; GRS Computational Biomedicine; IAS-5 Computational Biomedicine; INM-9 Jülich Supercomputing Center; JSC |
Published in: | Mass spectrometry reviews, 35 (2016) 1, S. 111 - 122 |
Imprint: |
New York, NY [u.a.]
Wiley
2016
|
PubMed ID: |
25952139 |
DOI: |
10.1002/mas.21465 |
Document Type: |
Journal Article |
Research Program: |
Theory, modelling and simulation Computational Science and Mathematical Methods |
Publikationsportal JuSER |
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. |