Journal
INTERNATIONAL JOURNAL OF MASS SPECTROMETRY
Volume 354, Issue -, Pages 288-291Publisher
ELSEVIER
DOI: 10.1016/j.ijms.2013.06.019
Keywords
Protein structure; Gas-phase vs. solution structure; Native ESI; Electron-capture dissociation (ECD); Top-down mass spectrometry
Funding
- National Institute of General Medical Sciences of the NIH [8 P41 GM103422-35]
- NSF [IBDR 0964199]
- NCRR [1S10 025101]
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The importance of protein and protein-complex structure motivates improvements in speed and sensitivity of structure determination in the gas phase and comparison with that in solution or solid state. An opportunity for the gas-phase measurement is mass spectrometry (MS) combined with native electrospray ionization (ESI), which delivers large proteins and protein complexes in their near-native states to the gas phase. In this communication, we describe the combination of native ESI, electron-capture dissociation (ECD), and top-down MS for exploring the structures of ubiquitin and cytochrome c in the gas phase and their relation to those in the solid-state and solution. We probe structure by comparing the protein's flexible regions, as predicted by the B-factor in X-ray crystallography, with the ECD fragments. The underlying hypothesis is that maintenance of structure gives fragments that can be predicted from B-factors. This strategy may be applicable in general when X-ray structures are available and extendable to the study of intrinsically disordered proteins. (C) 2013 Elsevier B.V. All rights reserved.
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