Enhanced Characterization of Membrane Protein Complexes by Ultraviolet Photodissociation Mass Spectrometry. Academic 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.

authors

• Laganowsky, Arthur

published proceedings

• Anal Chem

altmetric score

• 1.5

author list (cited authors)

• Sipe, S. N., Patrick, J. W., Laganowsky, A., & Brodbelt, J. S.

citation count

• 15

complete list of authors

• Sipe, Sarah N||Patrick, John W||Laganowsky, Arthur||Brodbelt, Jennifer S

publication date

• January 2020

publisher

• American Chemical Society (ACS)  Publisher

keywords

• Amino Acid Sequence
• Aquaporins
• Cation Transport Proteins
• Escherichia Coli
• Escherichia Coli Proteins
• Ion Channels
• Mass Spectrometry
• Models, Molecular
• Photolysis
• Protein Processing, Post-Translational
• Ultraviolet Rays

Digital Object Identifier (DOI)

• 10.1021/acs.analchem.9b03689

start page

• 899

end page

• 907

volume

• 92

issue

• 1

URL

• http://dx.doi.org/10.1021/acs.analchem.9b03689