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Collision cross sections for protein ions.

T Covey1, D J Douglas

  • 1Sciex, 55 Glen Cameron Road, L3T 1P2, Thornhill, Ontario, Canada.

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|November 15, 2013
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Summary
This summary is machine-generated.

This study introduces a new method to measure gas-phase protein ion cross sections using energy loss during collisions. Results show cross sections vary by protein size and charge, with potential solution conformation influences.

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Area of Science:

  • Mass spectrometry
  • Ion physics
  • Biophysical chemistry

Background:

  • Determining the size and shape of gas-phase protein ions is crucial for understanding their structure and interactions.
  • Existing methods for measuring ion cross sections can be complex and require specialized equipment.

Purpose of the Study:

  • To develop and validate a novel method for determining gas-phase protein ion cross sections.
  • To investigate the relationship between ion properties (size, charge) and their measured cross sections.
  • To explore the influence of solution origin on gas-phase ion conformation.

Main Methods:

  • A method based on ion energy loss through a collision gas was developed.
  • A simple model was used to relate energy loss to cross section.
  • Monte Carlo simulations were employed to validate the model.
  • Experimental cross sections were measured for several proteins: motilin, ubiquitin, cytochrome c, myoglobin, and bovine serum albumin.

Main Results:

  • Experimental cross sections were obtained, ranging from ~800 Å(2) for motilin to ~14,000 Å(2) for bovine serum albumin.
  • A general trend of increasing cross section with ion charge was observed.
  • Cytochrome c ions from aqueous solutions exhibited smaller cross sections compared to those from higher organic content solutions.

Conclusions:

  • The energy loss method provides a reliable approach for determining gas-phase protein ion cross sections.
  • Protein ion cross sections are influenced by factors such as size and charge.
  • Gas-phase protein ions may retain conformational information from their solution environment, impacting their measured cross sections.