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Accessing Different Protein Conformer Ensembles with Tunable Capillary Vibrating Sharp-Edge Spray Ionization.

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Capillary vibrating sharp-edge spray ionization (cVSSI) controls protein ion charge states and conformations. The study reveals how voltage affects ubiquitin ion distributions, offering insights into protein stability and mass spectrometry analysis.

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Area of Science:

  • Analytical Chemistry
  • Biochemistry
  • Physical Chemistry

Background:

  • Mass spectrometry (MS) is crucial for analyzing protein structure.
  • Controlling droplet charging in nebulized microdroplets impacts ion conformation.
  • Capillary vibrating sharp-edge spray ionization (cVSSI) offers tunable droplet charging.

Purpose of the Study:

  • To investigate the effect of voltage-controlled droplet charging using cVSSI on ubiquitin ion charge state distributions (CSDs) and conformations.
  • To understand the relationship between droplet dynamics, charge states, and protein conformer ensembles.
  • To explore cVSSI as a tool for studying protein stability.

Main Methods:

  • Utilized cVSSI to generate and analyze ubiquitin ions via mass spectrometry.
  • Varied applied voltage to establish distinct low-voltage (LV), mid-voltage (MV), and high-voltage (HV) regimes.
  • Analyzed charge state distributions (CSDs) and inferred protein conformations for each voltage regime.

Main Results:

  • LV regime (<+200 V) showed dominance of low charge states (2+-4+), linked to aerodynamic breakup and native conformations.
  • MV regime (+200 to +600 V) exhibited higher charge states (7+-12+), associated with droplet heating and partially unfolded species.
  • HV regime (>+600 V) achieved nano-electrospray ionization (nESI)-type distributions (5+, 6+ ions), indicating faster droplet charging and native conformation sampling.

Conclusions:

  • cVSSI enables precise control over droplet charging, influencing protein ion conformation and CSDs.
  • Different voltage regimes correlate with distinct droplet breakup pathways and resulting protein conformer ensembles.
  • cVSSI is a promising technique for investigating protein stability and conformational dynamics in mass spectrometry.