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PreprintCC BYChemRxiv

Mapping Protein Conformation Ensemble Transitions Using Capillary Vibrating Sharp-edge Spray Ionization and Native Mass Spectrometry

  • Mst Nigar Sultana1,2
  • Vikum K. Dewasurendra3,2
  • Mohammad Rahman1,2
  • Sultan Mahmud1,2
  • Sohag Ahmed1,2
  • Peng Li4,5
  • Matthew B. Johnson3,2
  • Stephen J. Valentine4,6
6 affiliations
  1. 1Department of Chemistry
  2. 2West Virginia University
  3. 3Department of Physics
  4. 4Chemistry
  5. 5Lehigh University
  6. 6University of Louisville
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Abstract

Capillary vibrating sharp-edge spray ionization (cVSSI) has been used to examine the effects of applied voltage and ion transfer tube temperature on the mass spectra recorded for ubiquitin ions. For positive polarity experiments, the results duplicate those described previously for one temperature setting where native protein conformer ensembles (N1 and N2) are formed at zero (and low) and high voltage settings and partially unfolded conformer ensembles (P) are formed in the middle voltage range. This work shows that the applied voltage cross over points between production of N1, P, and N2 ensembles shift with ion transfer tube temperature. Similarly, the voltage ranges associated with the presence of these conformer ensembles change with temperature as well. Additionally, the relative abundances of the ions comprising the conformer ensembles respond to ion transfer tube temperatures. Further experiments conducted in negative polarity mode reveal that the P ensemble is accessed for both positively- and negatively-charged ions in the mid voltage regime regardless of solution bias polarity. Taken together, the work supports the prior hypothesis that medium sized, moderately charged, and more slowly moving droplets produced by cVSSI undergo greater heating from the ion transfer tube leading to partial unfolding. The results are discussed with regard to future applications in highthroughput stability screening using “droplet charge tuning” with cVSSI.

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Cite

BibTeXRIS
BibTeX
@misc{sultana2026mapping,
  title = {{Mapping Protein Conformation Ensemble Transitions Using Capillary Vibrating Sharp-edge Spray Ionization and Native Mass Spectrometry}},
  author = {Mst Nigar Sultana and Vikum K. Dewasurendra and Mohammad Rahman and Sultan Mahmud and Sohag Ahmed and Peng Li and Matthew B. Johnson and Stephen J. Valentine},
  howpublished = {ChemRxiv},
  year = {2026},
  month = sep,
  doi = {10.26434/chemrxiv.15008465/v1},
  url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008465/v1},
  note = {CC BY},
}
RIS
TY  - UNPB
TI  - Mapping Protein Conformation Ensemble Transitions Using Capillary Vibrating Sharp-edge Spray Ionization and Native Mass Spectrometry
AU  - Mst Nigar Sultana
AU  - Vikum K. Dewasurendra
AU  - Mohammad Rahman
AU  - Sultan Mahmud
AU  - Sohag Ahmed
AU  - Peng Li
AU  - Matthew B. Johnson
AU  - Stephen J. Valentine
PY  - 2026
DA  - 2026/09/07
PB  - ChemRxiv
DO  - 10.26434/chemrxiv.15008465/v1
UR  - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15008465/v1
AB  - Capillary vibrating sharp-edge spray ionization (cVSSI) has been used to examine the effects of applied voltage and ion transfer tube temperature on the mass spectra recorded for ubiquitin ions. For positive polarity experiments, the results duplicate those described previously for one temperature setting where native protein conformer ensembles (N1 and N2) are formed at zero (and low) and high voltage settings and partially unfolded conformer ensembles (P) are formed in the middle voltage range. This work shows that the applied voltage cross over points between production of N1, P, and N2 ensembles shift with ion transfer tube temperature. Similarly, the voltage ranges associated with the presence of these conformer ensembles change with temperature as well. Additionally, the relative abundances of the ions comprising the conformer ensembles respond to ion transfer tube temperatures. Further experiments conducted in negative polarity mode reveal that the P ensemble is accessed for both positively- and negatively-charged ions in the mid voltage regime regardless of solution bias polarity. Taken together, the work supports the prior hypothesis that medium sized, moderately charged, and more slowly moving droplets produced by cVSSI undergo greater heating from the ion transfer tube leading to partial unfolding. The results are discussed with regard to future applications in highthroughput stability screening using “droplet charge tuning” with cVSSI.
ER  -