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Reference: Liko, Idlir, Allison, TM, Hopper, JTS et al., (2016). Negative Ions Enhance Survival of Membrane Protein Complexes. Journal of the American Society for Mass Spectrometry.Citable link to this page:

 

Negative Ions Enhance Survival of Membrane Protein Complexes

Abstract: Membrane protein complexes are commonly introduced to the mass spectrometer solubilized in detergent micelles. The collisional activation used to remove the detergent, however, often causes protein unfolding and dissociation. As in the case for soluble proteins, electrospray in the positive ion mode is most commonly used for the study of membrane proteins. Here we show several distinct advantages of employing the negative ion mode. Negative polarity can yield lower average charge states for membrane proteins solubilized in saccharide detergents, with enhanced peak resolution and reduced adduct formation. Most importantly, we demonstrate that negative ion mode electrospray ionization (ESI) minimizes subunit dissociation in the gas phase, allowing access to biologically relevant oligomeric states. Together, these properties mean that intact membrane protein ions can be generated in a greater range of solubilizing detergents. The formation of negative ions, therefore, greatly expands the possibilities of using mass spectrometry on this intractable class of protein.

Publication status:PublishedPeer Review status:Peer reviewedVersion:Publisher's versionDate of acceptance:2016-03-08Notes:© The Author(s), 2016. This article is published with open access at Springerlink.com.

Bibliographic Details

Publisher: Springer Verlag

Publisher Website: http://www.springerlink.com/?MUD=MP

Journal: Journal of the American Society for Mass Spectrometrysee more from them

Publication Website: http://link.springer.com/journal/13361

Volume: 27

Extent: 1099-1104

Issue Date: 2016-04-22Identifiers

Doi: https://doi.org/10.1007/s13361-016-1381-5

Issn: 1044-0305

Eissn: 1879-1123

Uuid: uuid:4ce3ed7b-0afe-4a93-9b3c-e0aeda76d668

Urn: uri:4ce3ed7b-0afe-4a93-9b3c-e0aeda76d668

Pubs-id: pubs:624863 Item Description

Type: journal-article;

Language: English

Version: Publisher's versionKeywords: Membrane proteins Structural biology Negative polarity

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Author: Liko, Idlir - Oxford, MPLS, Chemistry, Physical and Theoretical Chem - - - Allison, TM - - - Hopper, JTS - - - Benesch, Justin L.

Source: https://ora.ox.ac.uk/objects/uuid:4ce3ed7b-0afe-4a93-9b3c-e0aeda76d668



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