Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions
Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin result...
Ausführliche Beschreibung
Autor*in: |
Sterling, Harry J. [verfasserIn] |
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Format: |
Artikel |
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Sprache: |
Englisch |
Erschienen: |
2010 |
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Anmerkung: |
© American Society for Mass Spectrometry 2010 |
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Übergeordnetes Werk: |
Enthalten in: Journal of the American Society for Mass Spectrometry - Springer-Verlag, 1990, 21(2010), 10 vom: Okt., Seite 1762-1774 |
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Übergeordnetes Werk: |
volume:21 ; year:2010 ; number:10 ; month:10 ; pages:1762-1774 |
Links: |
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DOI / URN: |
10.1016/j.jasms.2010.06.012 |
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Katalog-ID: |
OLC2097685757 |
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520 | |a Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. | ||
650 | 4 | |a Charge State | |
650 | 4 | |a Electron Capture Dissociation | |
650 | 4 | |a Sulfolane | |
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700 | 1 | |a Daly, Michael P. |4 aut | |
700 | 1 | |a Feld, Geoffrey K. |4 aut | |
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700 | 1 | |a Kintzer, Alexander F. |4 aut | |
700 | 1 | |a Krantz, Bryan A. |4 aut | |
700 | 1 | |a Williams, Evan R. |4 aut | |
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10.1016/j.jasms.2010.06.012 doi (DE-627)OLC2097685757 (DE-He213)j.jasms.2010.06.012-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2010 Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. Charge State Electron Capture Dissociation Sulfolane High Charge State Arrival Time Distribution Daly, Michael P. aut Feld, Geoffrey K. aut Thoren, Katie L. aut Kintzer, Alexander F. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 21(2010), 10 vom: Okt., Seite 1762-1774 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:21 year:2010 number:10 month:10 pages:1762-1774 https://doi.org/10.1016/j.jasms.2010.06.012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2004 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 AR 21 2010 10 10 1762-1774 |
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10.1016/j.jasms.2010.06.012 doi (DE-627)OLC2097685757 (DE-He213)j.jasms.2010.06.012-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2010 Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. Charge State Electron Capture Dissociation Sulfolane High Charge State Arrival Time Distribution Daly, Michael P. aut Feld, Geoffrey K. aut Thoren, Katie L. aut Kintzer, Alexander F. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 21(2010), 10 vom: Okt., Seite 1762-1774 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:21 year:2010 number:10 month:10 pages:1762-1774 https://doi.org/10.1016/j.jasms.2010.06.012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2004 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 AR 21 2010 10 10 1762-1774 |
allfields_unstemmed |
10.1016/j.jasms.2010.06.012 doi (DE-627)OLC2097685757 (DE-He213)j.jasms.2010.06.012-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2010 Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. Charge State Electron Capture Dissociation Sulfolane High Charge State Arrival Time Distribution Daly, Michael P. aut Feld, Geoffrey K. aut Thoren, Katie L. aut Kintzer, Alexander F. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 21(2010), 10 vom: Okt., Seite 1762-1774 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:21 year:2010 number:10 month:10 pages:1762-1774 https://doi.org/10.1016/j.jasms.2010.06.012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2004 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 AR 21 2010 10 10 1762-1774 |
allfieldsGer |
10.1016/j.jasms.2010.06.012 doi (DE-627)OLC2097685757 (DE-He213)j.jasms.2010.06.012-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2010 Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. Charge State Electron Capture Dissociation Sulfolane High Charge State Arrival Time Distribution Daly, Michael P. aut Feld, Geoffrey K. aut Thoren, Katie L. aut Kintzer, Alexander F. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 21(2010), 10 vom: Okt., Seite 1762-1774 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:21 year:2010 number:10 month:10 pages:1762-1774 https://doi.org/10.1016/j.jasms.2010.06.012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2004 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 AR 21 2010 10 10 1762-1774 |
allfieldsSound |
10.1016/j.jasms.2010.06.012 doi (DE-627)OLC2097685757 (DE-He213)j.jasms.2010.06.012-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions 2010 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2010 Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. Charge State Electron Capture Dissociation Sulfolane High Charge State Arrival Time Distribution Daly, Michael P. aut Feld, Geoffrey K. aut Thoren, Katie L. aut Kintzer, Alexander F. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of the American Society for Mass Spectrometry Springer-Verlag, 1990 21(2010), 10 vom: Okt., Seite 1762-1774 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:21 year:2010 number:10 month:10 pages:1762-1774 https://doi.org/10.1016/j.jasms.2010.06.012 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-PHY SSG-OLC-CHE GBV_ILN_70 GBV_ILN_2004 GBV_ILN_4012 GBV_ILN_4125 GBV_ILN_4307 AR 21 2010 10 10 1762-1774 |
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Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions |
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effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions |
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Effects of supercharging reagents on noncovalent complex structure in electrospray ionization from aqueous solutions |
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Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. © American Society for Mass Spectrometry 2010 |
abstractGer |
Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. © American Society for Mass Spectrometry 2010 |
abstract_unstemmed |
Abstract The effects of two supercharging reagents, m-nitrobenzyl alcohol (m-NBA) and sulfolane, on the charge-state distributions and conformations of myoglobin ions formed by electrospray ionization were investigated. Addition of 0.4% m-NBA to aqueous ammonium acetate solutions of myoglobin results in an increase in the maximum charge state from 9+ to 19+, and an increase in the average charge state from 7.9+ to 11.7+, compared with solutions without m-NBA. The extent of supercharging with sulfolane on a per mole basis is lower than that with m-NBA, but comparable charging was obtained at higher concentration. Arrival time distributions obtained from traveling wave ion mobility spectrometry show that the higher charge state ions that are formed with these supercharging reagents are significantly more unfolded than lower charge state ions. Results from circular dichroism spectroscopy show that sulfolane can act as chemical denaturant, destabilizing myoglobin by ∼1.5 kcal/mol/M at 25 °C. Because these supercharging reagents have low vapor pressures, aqueous droplets are preferentially enriched in these reagents as evaporation occurs. Less evaporative cooling will occur after the droplets are substantially enriched in the low volatility supercharging reagent, and the droplet temperature should be higher compared with when these reagents are not present. Protein unfolding induced by chemical and/or thermal denaturation in the electrospray droplet appears to be the primary origin of the enhanced charging observed for noncovalent protein complexes formed from aqueous solutions that contain these supercharging reagents, although other factors almost certainly influence the extent of charging as well. © American Society for Mass Spectrometry 2010 |
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