Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations
Abstract The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI)...
Ausführliche Beschreibung
Autor*in: |
Sterling, Harry J. [verfasserIn] |
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Format: |
Artikel |
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Sprache: |
Englisch |
Erschienen: |
2011 |
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Anmerkung: |
© American Society for Mass Spectrometry 2011 |
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Übergeordnetes Werk: |
Enthalten in: Journal of The American Society for Mass Spectrometry - Springer-Verlag, 1990, 23(2011), 2 vom: 13. Dez., Seite 191-200 |
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Übergeordnetes Werk: |
volume:23 ; year:2011 ; number:2 ; day:13 ; month:12 ; pages:191-200 |
Links: |
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DOI / URN: |
10.1007/s13361-011-0301-y |
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Katalog-ID: |
OLC2097696554 |
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10.1007/s13361-011-0301-y doi (DE-627)OLC2097696554 (DE-He213)s13361-011-0301-y-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations 2011 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2011 Abstract The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI) solution can effectively increase the charge of concanavalin A dimers and tetramers, but at higher m-NBA concentrations, the increases in charge are accompanied by solution-phase dissociation of the dimers and up to a ~22% increase in the collision cross section (CCS) of the tetramers. With just 0.8% m-NBA added to the ESI solution of a ~630 kDa anthrax toxin octamer complex, the average charge is increased by only ~4% compared with the “native” complex, but it is sufficiently destabilized so that extensive gas-phase fragmentation occurs in the relatively high pressure regions of the TWIMS device. Anthrax toxin complexes exist in either a prechannel or a transmembrane channel state. With m-NBA, the prechannel state of the complex has the same CCS/charge ratio in the gas phase as the transmembrane channel state of the same complex formed without m-NBA, yet undergoes extensive dissociation, indicating that destabilization from supercharging occurs in the ESI droplet prior to ion formation and is not a result of Coulombic destabilization in the gas phase as a result of higher charging. These results demonstrate that the supercharging of large protein complexes is the result of conformational changes induced by the reagents in the ESI droplets, where enrichment of the supercharging reagent during droplet evaporation occurs. Kintzer, Alexander F. aut Feld, Geoffrey K. aut Cassou, Catherine A. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of The American Society for Mass Spectrometry Springer-Verlag, 1990 23(2011), 2 vom: 13. Dez., Seite 191-200 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:23 year:2011 number:2 day:13 month:12 pages:191-200 https://doi.org/10.1007/s13361-011-0301-y 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 23 2011 2 13 12 191-200 |
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10.1007/s13361-011-0301-y doi (DE-627)OLC2097696554 (DE-He213)s13361-011-0301-y-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations 2011 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2011 Abstract The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI) solution can effectively increase the charge of concanavalin A dimers and tetramers, but at higher m-NBA concentrations, the increases in charge are accompanied by solution-phase dissociation of the dimers and up to a ~22% increase in the collision cross section (CCS) of the tetramers. With just 0.8% m-NBA added to the ESI solution of a ~630 kDa anthrax toxin octamer complex, the average charge is increased by only ~4% compared with the “native” complex, but it is sufficiently destabilized so that extensive gas-phase fragmentation occurs in the relatively high pressure regions of the TWIMS device. Anthrax toxin complexes exist in either a prechannel or a transmembrane channel state. With m-NBA, the prechannel state of the complex has the same CCS/charge ratio in the gas phase as the transmembrane channel state of the same complex formed without m-NBA, yet undergoes extensive dissociation, indicating that destabilization from supercharging occurs in the ESI droplet prior to ion formation and is not a result of Coulombic destabilization in the gas phase as a result of higher charging. These results demonstrate that the supercharging of large protein complexes is the result of conformational changes induced by the reagents in the ESI droplets, where enrichment of the supercharging reagent during droplet evaporation occurs. Kintzer, Alexander F. aut Feld, Geoffrey K. aut Cassou, Catherine A. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of The American Society for Mass Spectrometry Springer-Verlag, 1990 23(2011), 2 vom: 13. Dez., Seite 191-200 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:23 year:2011 number:2 day:13 month:12 pages:191-200 https://doi.org/10.1007/s13361-011-0301-y 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 23 2011 2 13 12 191-200 |
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10.1007/s13361-011-0301-y doi (DE-627)OLC2097696554 (DE-He213)s13361-011-0301-y-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations 2011 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2011 Abstract The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI) solution can effectively increase the charge of concanavalin A dimers and tetramers, but at higher m-NBA concentrations, the increases in charge are accompanied by solution-phase dissociation of the dimers and up to a ~22% increase in the collision cross section (CCS) of the tetramers. With just 0.8% m-NBA added to the ESI solution of a ~630 kDa anthrax toxin octamer complex, the average charge is increased by only ~4% compared with the “native” complex, but it is sufficiently destabilized so that extensive gas-phase fragmentation occurs in the relatively high pressure regions of the TWIMS device. Anthrax toxin complexes exist in either a prechannel or a transmembrane channel state. With m-NBA, the prechannel state of the complex has the same CCS/charge ratio in the gas phase as the transmembrane channel state of the same complex formed without m-NBA, yet undergoes extensive dissociation, indicating that destabilization from supercharging occurs in the ESI droplet prior to ion formation and is not a result of Coulombic destabilization in the gas phase as a result of higher charging. These results demonstrate that the supercharging of large protein complexes is the result of conformational changes induced by the reagents in the ESI droplets, where enrichment of the supercharging reagent during droplet evaporation occurs. Kintzer, Alexander F. aut Feld, Geoffrey K. aut Cassou, Catherine A. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of The American Society for Mass Spectrometry Springer-Verlag, 1990 23(2011), 2 vom: 13. Dez., Seite 191-200 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:23 year:2011 number:2 day:13 month:12 pages:191-200 https://doi.org/10.1007/s13361-011-0301-y 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 23 2011 2 13 12 191-200 |
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10.1007/s13361-011-0301-y doi (DE-627)OLC2097696554 (DE-He213)s13361-011-0301-y-p DE-627 ger DE-627 rakwb eng 530 VZ 11 ssgn Sterling, Harry J. verfasserin aut Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations 2011 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © American Society for Mass Spectrometry 2011 Abstract The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI) solution can effectively increase the charge of concanavalin A dimers and tetramers, but at higher m-NBA concentrations, the increases in charge are accompanied by solution-phase dissociation of the dimers and up to a ~22% increase in the collision cross section (CCS) of the tetramers. With just 0.8% m-NBA added to the ESI solution of a ~630 kDa anthrax toxin octamer complex, the average charge is increased by only ~4% compared with the “native” complex, but it is sufficiently destabilized so that extensive gas-phase fragmentation occurs in the relatively high pressure regions of the TWIMS device. Anthrax toxin complexes exist in either a prechannel or a transmembrane channel state. With m-NBA, the prechannel state of the complex has the same CCS/charge ratio in the gas phase as the transmembrane channel state of the same complex formed without m-NBA, yet undergoes extensive dissociation, indicating that destabilization from supercharging occurs in the ESI droplet prior to ion formation and is not a result of Coulombic destabilization in the gas phase as a result of higher charging. These results demonstrate that the supercharging of large protein complexes is the result of conformational changes induced by the reagents in the ESI droplets, where enrichment of the supercharging reagent during droplet evaporation occurs. Kintzer, Alexander F. aut Feld, Geoffrey K. aut Cassou, Catherine A. aut Krantz, Bryan A. aut Williams, Evan R. aut Enthalten in Journal of The American Society for Mass Spectrometry Springer-Verlag, 1990 23(2011), 2 vom: 13. Dez., Seite 191-200 (DE-627)130977357 (DE-600)1073671-2 (DE-576)277732093 1044-0305 nnns volume:23 year:2011 number:2 day:13 month:12 pages:191-200 https://doi.org/10.1007/s13361-011-0301-y 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 23 2011 2 13 12 191-200 |
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Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations |
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Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations |
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Sterling, Harry J. |
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Journal of The American Society for Mass Spectrometry |
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Journal of The American Society for Mass Spectrometry |
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Sterling, Harry J. Kintzer, Alexander F. Feld, Geoffrey K. Cassou, Catherine A. Krantz, Bryan A. Williams, Evan R. |
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supercharging protein complexes from aqueous solution disrupts their native conformations |
title_auth |
Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations |
abstract |
Abstract The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI) solution can effectively increase the charge of concanavalin A dimers and tetramers, but at higher m-NBA concentrations, the increases in charge are accompanied by solution-phase dissociation of the dimers and up to a ~22% increase in the collision cross section (CCS) of the tetramers. With just 0.8% m-NBA added to the ESI solution of a ~630 kDa anthrax toxin octamer complex, the average charge is increased by only ~4% compared with the “native” complex, but it is sufficiently destabilized so that extensive gas-phase fragmentation occurs in the relatively high pressure regions of the TWIMS device. Anthrax toxin complexes exist in either a prechannel or a transmembrane channel state. With m-NBA, the prechannel state of the complex has the same CCS/charge ratio in the gas phase as the transmembrane channel state of the same complex formed without m-NBA, yet undergoes extensive dissociation, indicating that destabilization from supercharging occurs in the ESI droplet prior to ion formation and is not a result of Coulombic destabilization in the gas phase as a result of higher charging. These results demonstrate that the supercharging of large protein complexes is the result of conformational changes induced by the reagents in the ESI droplets, where enrichment of the supercharging reagent during droplet evaporation occurs. © American Society for Mass Spectrometry 2011 |
abstractGer |
Abstract The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI) solution can effectively increase the charge of concanavalin A dimers and tetramers, but at higher m-NBA concentrations, the increases in charge are accompanied by solution-phase dissociation of the dimers and up to a ~22% increase in the collision cross section (CCS) of the tetramers. With just 0.8% m-NBA added to the ESI solution of a ~630 kDa anthrax toxin octamer complex, the average charge is increased by only ~4% compared with the “native” complex, but it is sufficiently destabilized so that extensive gas-phase fragmentation occurs in the relatively high pressure regions of the TWIMS device. Anthrax toxin complexes exist in either a prechannel or a transmembrane channel state. With m-NBA, the prechannel state of the complex has the same CCS/charge ratio in the gas phase as the transmembrane channel state of the same complex formed without m-NBA, yet undergoes extensive dissociation, indicating that destabilization from supercharging occurs in the ESI droplet prior to ion formation and is not a result of Coulombic destabilization in the gas phase as a result of higher charging. These results demonstrate that the supercharging of large protein complexes is the result of conformational changes induced by the reagents in the ESI droplets, where enrichment of the supercharging reagent during droplet evaporation occurs. © American Society for Mass Spectrometry 2011 |
abstract_unstemmed |
Abstract The effects of aqueous solution supercharging on the solution- and gas-phase structures of two protein complexes were investigated using traveling-wave ion mobility-mass spectrometry (TWIMS-MS). Low initial concentrations of m-nitrobenzyl alcohol (m-NBA) in the electrospray ionization (ESI) solution can effectively increase the charge of concanavalin A dimers and tetramers, but at higher m-NBA concentrations, the increases in charge are accompanied by solution-phase dissociation of the dimers and up to a ~22% increase in the collision cross section (CCS) of the tetramers. With just 0.8% m-NBA added to the ESI solution of a ~630 kDa anthrax toxin octamer complex, the average charge is increased by only ~4% compared with the “native” complex, but it is sufficiently destabilized so that extensive gas-phase fragmentation occurs in the relatively high pressure regions of the TWIMS device. Anthrax toxin complexes exist in either a prechannel or a transmembrane channel state. With m-NBA, the prechannel state of the complex has the same CCS/charge ratio in the gas phase as the transmembrane channel state of the same complex formed without m-NBA, yet undergoes extensive dissociation, indicating that destabilization from supercharging occurs in the ESI droplet prior to ion formation and is not a result of Coulombic destabilization in the gas phase as a result of higher charging. These results demonstrate that the supercharging of large protein complexes is the result of conformational changes induced by the reagents in the ESI droplets, where enrichment of the supercharging reagent during droplet evaporation occurs. © American Society for Mass Spectrometry 2011 |
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title_short |
Supercharging Protein Complexes from Aqueous Solution Disrupts their Native Conformations |
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Kintzer, Alexander F. Feld, Geoffrey K. Cassou, Catherine A. Krantz, Bryan A. Williams, Evan R. |
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