Surface induced dissociation as a tool to study membrane protein complexes

Sophie R Harvey; Yang Liu; Wen Liu; Vicki H Wysocki; Arthur Laganowsky

doi:10.1039/c6cc09606a

Surface induced dissociation as a tool to study membrane protein complexes

Chem Commun (Camb). 2017 Mar 9;53(21):3106-3109. doi: 10.1039/c6cc09606a.

Authors

Sophie R Harvey¹, Yang Liu², Wen Liu², Vicki H Wysocki³, Arthur Laganowsky⁴

Affiliations

¹ The Department of Chemistry and Biochemistry, The Ohio State University, 460 W 12th Avenue, Columbus, Ohio 43210, USA. wysocki.11@osu.edu and School of Chemistry, Manchester Institute of Biotechnology, University of Manchester, Manchester, M1 7DN, UK.
² Institute of Biosciences and Technology, Texas A&M Health Science Center, Houston, Texas 77030, USA. alaganowsky@ibt.tamhsc.edu.
³ The Department of Chemistry and Biochemistry, The Ohio State University, 460 W 12th Avenue, Columbus, Ohio 43210, USA. wysocki.11@osu.edu.
⁴ Institute of Biosciences and Technology, Texas A&M Health Science Center, Houston, Texas 77030, USA. alaganowsky@ibt.tamhsc.edu and Department of Chemistry, Texas A&M University, College Station, Texas 77843, USA.

Abstract

Native ion mobility mass spectrometry (MS) and surface induced dissociation (SID) are applied to study the integral membrane protein complexes AmtB and AqpZ. Fragments produced from SID are consistent with the solved structures of these complexes. SID is, therefore, a promising tool for characterization of membrane protein complexes.

MeSH terms

Aquaporins / chemistry*
Cation Transport Proteins / chemistry*
Escherichia coli Proteins / chemistry*
Mass Spectrometry
Membrane Proteins / chemistry*
Surface Properties

Substances

AmtB protein, E coli
Aquaporins
Cation Transport Proteins
Escherichia coli Proteins
Membrane Proteins
aqpZ protein, E coli

Abstract

MeSH terms

Substances

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