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Title
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Proton dynamics in protein mass spectrometry
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Author
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Abstract
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| Native electrospray ionization/ion mobility-mass spectrometry (ESI/IM-MS) allows an accurate determination of low-resolution structural features of proteins. Yet, the presence of proton dynamics, observed already by us for DNA in the gas phase, and its impact on protein structural determinants, have not been investigated so far. Here, we address this issue by a multistep simulation strategy on a pharmacologically relevant peptide, the N-terminal residues of amyloid-(beta) peptide (A(beta)(1-16)). Our calculations reproduce the experimental maximum charge state from ESIMS and are also in fair agreement with collision cross section (CCS) data measured here by ESI/IM-MS. Although the main structural features are preserved, subtle conformational changes do take place in the first similar to 0.1 ms of dynamics. In addition, intramolecular proton dynamics processes occur on the picosecond-time scale in the gas phase as emerging from quantum mechanics/molecular mechanics (QM/MM) simulations at the B3LYP level of theory. We conclude that proton transfer phenomena do occur frequently during fly time in ESI-MS experiments (typically on the millisecond time scale). However, the structural changes associated with the process do not significantly affect the structural determinants. |
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Language
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English
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Source (journal)
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The journal of physical chemistry letters / American Chemical Society. - Washington, D.C, 2010, currens
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Publication
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Washington, D.C
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American Chemical Society
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2017
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ISSN
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1948-7185
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DOI
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10.1021/ACS.JPCLETT.7B00127
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Volume/pages
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8
:6
(2017)
, p. 1105-1112
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ISI
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000396975600001
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Pubmed ID
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28207277
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Full text (Publisher's DOI)
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Full text (open access)
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