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Surface-Induced Dissociation for Protein Complex Characterization.

Sophie R Harvey1, Gili Ben-Nissan2, Michal Sharon2

  • 1Department of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH, USA.

Methods in Molecular Biology (Clifton, N.J.)
|June 3, 2022
PubMed
Summary
This summary is machine-generated.

Native mass spectrometry (nMS) coupled with surface-induced dissociation (SID) characterizes protein complexes. This powerful technique reveals subunit connectivity and arrangements, even for unknown structures, advancing proteoform analysis.

Keywords:
High-resolution mass spectrometryNative mass spectrometryProtein complexProtein mass spectrometryProteoform identificationSurface-induced dissociation

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Structural Biology

Background:

  • Native mass spectrometry (nMS) allows the study of intact non-covalent complexes in the gas phase.
  • nMS provides insights into protein complex composition, stoichiometry, and topology.
  • Surface-induced dissociation (SID) can be coupled with nMS to determine subunit connectivity.

Purpose of the Study:

  • To describe the characterization of protein complexes using nMS and SID.
  • To demonstrate the utility of nMS-SID for obtaining substructural information and subunit connectivity.
  • To highlight the potential of SID for analyzing proteoforms.

Main Methods:

  • Characterization of protein complexes using native mass spectrometry (nMS).
  • Application of surface-induced dissociation (SID) coupled with nMS for substructural analysis.
  • Focus on SID implementation within a Q Exactive UHMR instrument and its commercial availability.

Main Results:

  • Substructural information obtained via nMS-SID is consistent with known complex structures.
  • The method provides confidence in elucidating subunit connectivity and arrangements for unknown complexes.
  • High-energy SID yields information regarding the presence of various proteoforms.

Conclusions:

  • nMS coupled with SID is a valuable method for characterizing protein complexes.
  • This technique offers insights into subunit connectivity and arrangements, aiding in the structural determination of unknown complexes.
  • Ongoing efforts aim to broaden the accessibility of SID technology on multiple platforms.