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Trajectory taken by dimeric Cu/Zn superoxide dismutase through the protein unfolding and dissociation landscape Is modulated by salt bridge formation

Abstract:

Native mass spectrometry (MS) is a powerful means for studying macromolecular protein assemblies, including accessing activated states. However, much remains to be understood about what governs which regions of the protein (un)folding funnel, which can be explored by activation of protein ions in a vacuum. Here, we examine the trajectory that Cu/Zn superoxide dismutase (SOD1) dimers take over the unfolding and dissociation free energy landscape in a vacuum. We examined wild-type SOD1 and six ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/acs.analchem.9b01699

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Role:
Author
ORCID:
0000-0002-1764-3809
Publisher:
American Chemical Society
Journal:
Analytical Chemistry More from this journal
Volume:
92
Issue:
2
Pages:
1702-1711
Publication date:
2019-12-19
Acceptance date:
2019-12-19
DOI:
EISSN:
1520-6882
ISSN:
0003-2700
Pmid:
31854977
Language:
English
Keywords:
Pubs id:
1081503
Local pid:
pubs:1081503
Deposit date:
2020-02-07

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