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Title: Size Exclusion Chromatography-Ion Mobility-Mass Spectrometry Coupling: a Step Toward Structural Biology

Abstract

Noncovalent interactions are essential for the structural organization of biomacromolecules in cells. For this reason, the study of the biophysical, dynamic, and architectural interactions among biomacromolecules is essential. Since mass spectrometry requires compatible solutions while preserving the noncovalent bonding network, we envisioned that size exclusion chromatography coupled with ion mobility and mass spectrometry would be a valuable technique to desalt the initial sample and provide solution and gas-phase structural information in a single stage experiment. Such coupling allowed obtaining information on solution protein complex composition with SEC separation and on authenticity and purity with IMS-MS. Our study demonstrated that such coupling is compatible, useful, as well as suitable for a routine analysis, in pharmaceutical industry, for example. Mobility data were reliable and injected standards allowed calibrating the collision cross-section scale. .

Authors:
;  [1]
  1. Université Paris Sud-CNRS, UMR 8000, Rue Henri Becquerel (France)
Publication Date:
OSTI Identifier:
22776823
Resource Type:
Journal Article
Journal Name:
Journal of the American Society for Mass Spectrometry
Additional Journal Information:
Journal Volume: 28; Journal Issue: 11; Other Information: Copyright (c) 2017 American Society for Mass Spectrometry; http://www.springer-ny.com; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1044-0305
Country of Publication:
United States
Language:
English
Subject:
46 INSTRUMENTATION RELATED TO NUCLEAR SCIENCE AND TECHNOLOGY; BIOLOGY; COLLISIONS; CROSS SECTIONS; INTERACTIONS; ION MOBILITY; MASS SPECTROSCOPY; PROTEINS

Citation Formats

Rest, Guillaume Van der, and Halgand, Frédéric. Size Exclusion Chromatography-Ion Mobility-Mass Spectrometry Coupling: a Step Toward Structural Biology. United States: N. p., 2017. Web. doi:10.1007/S13361-017-1810-0.
Rest, Guillaume Van der, & Halgand, Frédéric. Size Exclusion Chromatography-Ion Mobility-Mass Spectrometry Coupling: a Step Toward Structural Biology. United States. doi:10.1007/S13361-017-1810-0.
Rest, Guillaume Van der, and Halgand, Frédéric. Wed . "Size Exclusion Chromatography-Ion Mobility-Mass Spectrometry Coupling: a Step Toward Structural Biology". United States. doi:10.1007/S13361-017-1810-0.
@article{osti_22776823,
title = {Size Exclusion Chromatography-Ion Mobility-Mass Spectrometry Coupling: a Step Toward Structural Biology},
author = {Rest, Guillaume Van der and Halgand, Frédéric},
abstractNote = {Noncovalent interactions are essential for the structural organization of biomacromolecules in cells. For this reason, the study of the biophysical, dynamic, and architectural interactions among biomacromolecules is essential. Since mass spectrometry requires compatible solutions while preserving the noncovalent bonding network, we envisioned that size exclusion chromatography coupled with ion mobility and mass spectrometry would be a valuable technique to desalt the initial sample and provide solution and gas-phase structural information in a single stage experiment. Such coupling allowed obtaining information on solution protein complex composition with SEC separation and on authenticity and purity with IMS-MS. Our study demonstrated that such coupling is compatible, useful, as well as suitable for a routine analysis, in pharmaceutical industry, for example. Mobility data were reliable and injected standards allowed calibrating the collision cross-section scale. .},
doi = {10.1007/S13361-017-1810-0},
journal = {Journal of the American Society for Mass Spectrometry},
issn = {1044-0305},
number = 11,
volume = 28,
place = {United States},
year = {2017},
month = {11}
}