Electron capture dissociation mass spectrometry of peptide cations containing a lysine homologue: a mobile proton model for explaining the observation of b-type product ions

The structural analysis of sulfated carbohydrates such as glycosaminoglycans (GAGs) has been a long-standing challenge for the field of mass spectrometry. The dissociation of sulfated carbohydrates by collisionally-activated dissociation (CAD) or infrared multiphoton dissociation (IRMPD), which activate ions via vibrational excitation, typically result in few cleavages and abundant SO3 loss for highly sulfated GAGs such as heparin and heparan sulfate, hampering efforts to determine sites of modification. The recent application of electron activation techniques, specifically electron capture dissociation (ECD) and electron detachment dissociation (EDD), provides a marked improvement for the mass spectrometry characterization of GAGs. In this work, we compare ECD, EDD and IRMPD for the dissociation of the highly sulfated carbohydrate sucrose octasulfate (SOS). Both positive and negative multiply-charged ions are investigated. ECD, EDD and IRMPD of SOS produce abundant and reproducible fragmentation. The product ions produced by ECD are quite different than those produced by IRMPD of SOS positive ions, suggesting different dissociation mechanisms as a result of electronic versus vibrational excitation. The product ions produced by EDD and IRMPD of SOS negative ions also differ from each other. Evidence for SO3 rearrangement exists in the negative ion IRMPD data, complicating the assignment of product ions.

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Proteoform Differentiation using Tandem Trapped Ion Mobility, Electron Capture Dissociation, and ToF Mass Spectrometry

Analytical Chemistry ◽

10.1021/acs.analchem.1c01735 ◽

2021 ◽

Author(s):

Kevin Jeanne Dit Fouque ◽

Desmond Kaplan ◽

Valery G. Voinov ◽

Frederik H. V. Holck ◽

Ole N. Jensen ◽

...

Keyword(s):

Mass Spectrometry ◽

Electron Capture ◽

Electron Capture Dissociation ◽

Ion Mobility ◽

Trapped Ion

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Electron Capture Dissociation Implementation Progress in Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Journal of the American Society for Mass Spectrometry ◽

10.1016/j.jasms.2008.02.007 ◽

2008 ◽

Vol 19 (6) ◽

pp. 762-771 ◽

Cited By ~ 27

Author(s):

Yury O. Tsybin ◽

John P. Quinn ◽

Oleg Yu Tsybin ◽

Christopher L. Hendrickson ◽

Alan G. Marshall

Keyword(s):

Mass Spectrometry ◽

Fourier Transform ◽

Electron Capture ◽

Electron Capture Dissociation ◽

Cyclotron Resonance ◽

Ion Cyclotron Resonance ◽

Ion Cyclotron ◽

Implementation Progress

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Secondary and tertiary structures of gaseous protein ions characterized by electron capture dissociation mass spectrometry and photofragment spectroscopy

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.212643599 ◽

2002 ◽

Vol 99 (25) ◽

pp. 15863-15868 ◽

Cited By ~ 168

Author(s):

H. Oh ◽

K. Breuker ◽

S. K. Sze ◽

Y. Ge ◽

B. K. Carpenter ◽

...

Keyword(s):

Mass Spectrometry ◽

Electron Capture ◽

Electron Capture Dissociation ◽

Tertiary Structures ◽

Protein Ions

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Electron capture dissociation and drift tube ion mobility-mass spectrometry coupled with site directed mutations provide insights into the conformational diversity of a metamorphic protein

Physical Chemistry Chemical Physics ◽

10.1039/c4cp05136j ◽

2015 ◽

Vol 17 (16) ◽

pp. 10538-10550 ◽

Cited By ~ 10

Author(s):

Sophie R. Harvey ◽

Massimiliano Porrini ◽

Robert C. Tyler ◽

Cait E. MacPhee ◽

Brian F. Volkman ◽

...

Keyword(s):

Mass Spectrometry ◽

Electron Capture ◽

Electron Capture Dissociation ◽

Ion Mobility ◽

Drift Tube ◽

Ion Mobility Mass Spectrometry ◽

Top Down ◽

Conformational Diversity ◽

Metamorphic Protein

Ion mobility mass spectrometry can be combined with data from top-down sequencing to discern adopted conformations of proteins in the absence of solvent.

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