Gas-phase dissociation pathways of a tetrameric protein complex
The gas-phase dissociation of the tetrameric complex transthyretin (TTR) has been investigated with tandem-mass spectrometry (tandem-MS) using a nanoflow-electrospray interface and a quadrupole time-of-flight (Q-TOF) mass spectrometer. The results show that highly charged monomeric product ions diss...
Main Authors: | , , |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2003
|
_version_ | 1797089818993229824 |
---|---|
author | Sobott, F McCammon, MG Robinson, C |
author_facet | Sobott, F McCammon, MG Robinson, C |
author_sort | Sobott, F |
collection | OXFORD |
description | The gas-phase dissociation of the tetrameric complex transthyretin (TTR) has been investigated with tandem-mass spectrometry (tandem-MS) using a nanoflow-electrospray interface and a quadrupole time-of-flight (Q-TOF) mass spectrometer. The results show that highly charged monomeric product ions dissociate from the macromolecular complex to form trimeric products. Manipulating the pressure conditions within the mass spectrometer facilitates the formation of metastable ions. These were observed for the transitions from tetrameric to monomeric and trimeric product ions and additionally for losses of small molecules associated with the protein complex in the gas phase. These results are interpreted in the light of recent mechanisms for the electrospray process and provide insight into the composition and factors governing the stability of macromolecular ions in the gas phase. © 2003 Elsevier B.V. All rights reserved. |
first_indexed | 2024-03-07T03:09:34Z |
format | Journal article |
id | oxford-uuid:b3b78de3-475e-4a6f-9aa0-e79e3ab3049f |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T03:09:34Z |
publishDate | 2003 |
record_format | dspace |
spelling | oxford-uuid:b3b78de3-475e-4a6f-9aa0-e79e3ab3049f2022-03-27T04:21:16ZGas-phase dissociation pathways of a tetrameric protein complexJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b3b78de3-475e-4a6f-9aa0-e79e3ab3049fEnglishSymplectic Elements at Oxford2003Sobott, FMcCammon, MGRobinson, CThe gas-phase dissociation of the tetrameric complex transthyretin (TTR) has been investigated with tandem-mass spectrometry (tandem-MS) using a nanoflow-electrospray interface and a quadrupole time-of-flight (Q-TOF) mass spectrometer. The results show that highly charged monomeric product ions dissociate from the macromolecular complex to form trimeric products. Manipulating the pressure conditions within the mass spectrometer facilitates the formation of metastable ions. These were observed for the transitions from tetrameric to monomeric and trimeric product ions and additionally for losses of small molecules associated with the protein complex in the gas phase. These results are interpreted in the light of recent mechanisms for the electrospray process and provide insight into the composition and factors governing the stability of macromolecular ions in the gas phase. © 2003 Elsevier B.V. All rights reserved. |
spellingShingle | Sobott, F McCammon, MG Robinson, C Gas-phase dissociation pathways of a tetrameric protein complex |
title | Gas-phase dissociation pathways of a tetrameric protein complex |
title_full | Gas-phase dissociation pathways of a tetrameric protein complex |
title_fullStr | Gas-phase dissociation pathways of a tetrameric protein complex |
title_full_unstemmed | Gas-phase dissociation pathways of a tetrameric protein complex |
title_short | Gas-phase dissociation pathways of a tetrameric protein complex |
title_sort | gas phase dissociation pathways of a tetrameric protein complex |
work_keys_str_mv | AT sobottf gasphasedissociationpathwaysofatetramericproteincomplex AT mccammonmg gasphasedissociationpathwaysofatetramericproteincomplex AT robinsonc gasphasedissociationpathwaysofatetramericproteincomplex |