The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes

The application of ion-mobility mass spectrometry for structure/function investigation of protein... Available online at www.sciencedirect.com ScienceDirect The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes Gili Ben-Nissan and Michal Sharon Ion-mobility mass spectrometry (IM-MS) is an approach that IM-MS is a method that couples MS measurements with can provide information on the stoichiometry, composition, IM separation (recent reviews include [6–13]). By means protein contacts and topology of protein complexes. The of this method, the time it takes for a protein (or its various power of this approach lies not only in its sensitivity and speed populated structural states) to transverse a weak electrical of analysis, but also in the fact that it is a technique that can gradient in a gas-filled chamber is measured. The drift capture the repertoire of conformational states adopted by time depends not only on the mass and charge, but also on protein assemblies. Here, we describe the array of available IM- the shape of the analyzed protein complex. Larger ions MS based tools, and demonstrate their application to the collide more frequently with the neutral gas, hindering structural characterization of various protein complexes, their progress and therefore increasing their drift time including challenging systems as amyloid aggregates and relative to more compact http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Chemical Biology Elsevier

The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes

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Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier Ltd
ISSN
1367-5931
D.O.I.
10.1016/j.cbpa.2017.10.026
Publisher site
See Article on Publisher Site

Abstract

Available online at www.sciencedirect.com ScienceDirect The application of ion-mobility mass spectrometry for structure/function investigation of protein complexes Gili Ben-Nissan and Michal Sharon Ion-mobility mass spectrometry (IM-MS) is an approach that IM-MS is a method that couples MS measurements with can provide information on the stoichiometry, composition, IM separation (recent reviews include [6–13]). By means protein contacts and topology of protein complexes. The of this method, the time it takes for a protein (or its various power of this approach lies not only in its sensitivity and speed populated structural states) to transverse a weak electrical of analysis, but also in the fact that it is a technique that can gradient in a gas-filled chamber is measured. The drift capture the repertoire of conformational states adopted by time depends not only on the mass and charge, but also on protein assemblies. Here, we describe the array of available IM- the shape of the analyzed protein complex. Larger ions MS based tools, and demonstrate their application to the collide more frequently with the neutral gas, hindering structural characterization of various protein complexes, their progress and therefore increasing their drift time including challenging systems as amyloid aggregates and relative to more compact

Journal

Current Opinion in Chemical BiologyElsevier

Published: Feb 1, 2018

References

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