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Reference: Liko, I, Allison, TM, Hopper et al., (2016). Negative ions enhance survival of membrane protein complexes. Journal of the American Society for Mass Spectrometry, 27 (6), 1099-1104.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.

Peer Review status:Peer reviewedPublication status:PublishedVersion:Publisher's versionNotes:Copyright © 2016 The Author(s). This article is distributed under the terms of the CreativeCommons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricteduse, distribution, and reproduction in any medium,provided you give appropriate credit to the original author(s)and the source, provide a link to the Creative Commonslicense, and indicate if changes were made.

Bibliographic Details

Publisher: Springer US

Publisher Website: http://www.springer.com/

Publisher: Springer Verlag (Germany)

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

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

Issue Date: 2016

pages:1099-1104Identifiers

Urn: uuid:75a878dc-ee9d-45c0-b3da-e91ea5a849b9

Source identifier: 624863

Eissn: 1879-1123

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

Issn: 1044-0305 Item Description

Type: Journal article;

Language: English

Version: Publisher's versionKeywords: Membrane proteins Structural biology Negative polarity Tiny URL: pubs:624863

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Author: Liko, I - institutionUniversity of Oxford Oxford, MPLS, Chemistry, Physical and Theoretical Chem - - - Allison, TM - institutionU

Source: https://ora.ox.ac.uk/objects/uuid:75a878dc-ee9d-45c0-b3da-e91ea5a849b9



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