Work

Enhanced Characterization of Membrane Protein Complexes by Ultraviolet Photodissociation Mass Spectrometry

Year: 2019

Type: article

Abstract: Development of chemical chaperones to solubilize membrane protein complexes in aqueous solutions has allowed for gas-phase analysis of their native-like assemblies, including rapid evaluation of stability and interacting partners. Characterization of protein primary sequence, however, has thus far been limited. Ultraviolet photodissociation (UVPD) generates a multitude of sequence ions for the E. coli ammonia channel (AmtB), provides improved localization of a possible post-translational modification of aquaporin Z (AqpZ), and surpasses previous reports of sequence coverage for mechanosensitive channel of large conductance (MscL). Variations in UVPD sequence ion abundance have been shown to correspond to structural changes induced upon some perturbation. Preliminary results are reported here for elucidating increased rigidity or flexibility of MscL when bound to various phospholipids.

Source: Analytical Chemistry

DOI: 10.1021/acs.analchem.9b03689

Authors: Sarah N. Sipe, John W. Patrick, Arthur Laganowsky, Jennifer S. Brodbelt

Institutions: The University of Texas at Austin, Texas A&M University

Language: English

Topic: Mass Spectrometry Techniques and Applications

Subfield: Spectroscopy

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: Welch Foundation, National Institute of General Medical Sciences

Awards: Native ion mobility mass spectrometry studies of potassium inward rectifier channels: insight into gating and lipid binding, G4226750041, UVPD Mass Spectrometry of Protein Complexes