Ion Mobility-Mass Spectrometry Reveals Highly-Compact Intermediates in the Collision Induced Dissociation of Charge-Reduced Protein Complexes

Journal of the American Society for Mass Spectrometry
Russell E BornscheinBrandon T Ruotolo

Abstract

Protocols that aim to construct complete models of multiprotein complexes based on ion mobility and mass spectrometry data are becoming an important element of integrative structural biology efforts. However, the usefulness of such data is predicated, in part, on an ability to measure individual subunits removed from the complex while maintaining a compact/folded state. Gas-phase dissociation of intact complexes using collision induced dissociation is a potentially promising pathway for acquiring such protein monomer size information, but most product ions produced are possessed of high charge states and elongated/string-like conformations that are not useful in protein complex modeling. It has previously been demonstrated that the collision induced dissociation of charge-reduced protein complexes can produce compact subunit product ions; however, their formation mechanism is not well understood. Here, we present new experimental evidence for the avidin (64 kDa) and aldolase (157 kDa) tetramers that demonstrates significant complex remodeling during the dissociation of charge-reduced assemblies. Detailed analysis and modeling indicates that highly compact intermediates are accessed during the dissociation process by both comple...Continue Reading

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Citations

Dec 1, 2017·European Journal of Mass Spectrometry·Yelena YefremovaMichael O Glocker
Dec 14, 2018·Journal of the American Society for Mass Spectrometry·Jean R N HalerEdwin De Pauw
Jul 12, 2021·Biochimica Et Biophysica Acta. Proteins and Proteomics·Kirsty SkeeneCris Lapthorn
Nov 3, 2021·Chemical Reviews·Dalton T SnyderVicki H Wysocki

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