Conformational effects in protein electrospray-ionization mass spectrometry.
| Autor: | Li J; Computational Biophysics, German Research School for Simulation Sciences, and Computational Biomedicine, Institute for Advanced Simulation IAS-5 and Institute of Neuroscience and Medicine INM-9, Forschungszentrum Jülich, 52425 Jülich, Germany.; Institute of Biochemistry and Molecular Biology, RWTH Aachen University, 52057 Aachen, Germany., Santambrogio C; Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy., Brocca S; Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy., Rossetti G; Computational Biophysics, German Research School for Simulation Sciences, and Computational Biomedicine, Institute for Advanced Simulation IAS-5 and Institute of Neuroscience and Medicine INM-9, Forschungszentrum Jülich, 52425 Jülich, Germany.; Jülich Supercomputing Centre, Forschungszentrum Jülich, 52425 Jülich, Germany., Carloni P; Computational Biophysics, German Research School for Simulation Sciences, and Computational Biomedicine, Institute for Advanced Simulation IAS-5 and Institute of Neuroscience and Medicine INM-9, Forschungszentrum Jülich, 52425 Jülich, Germany., Grandori R; Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy. |
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| Jazyk: | angličtina |
| Zdroj: | Mass spectrometry reviews [Mass Spectrom Rev] 2016 Jan-Feb; Vol. 35 (1), pp. 111-22. Date of Electronic Publication: 2015 May 07. |
| DOI: | 10.1002/mas.21465 |
| Abstrakt: | 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. (© 2015 Wiley Periodicals, Inc.) |
| Databáze: | MEDLINE |
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