Top-down hydrogen/deuterium exchange and ECD-stitched FTICR-MS for probing structural dynamics of a 29-kDa enzyme

2012 ◽  
Vol 325-327 ◽  
pp. 130-138 ◽  
Author(s):  
Jingxi Pan ◽  
Jun Han ◽  
Christoph H. Borchers
Keyword(s):  
Structural Dynamics ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Top Down ◽  
Fticr Ms ◽  
Hydrogen Deuterium

scholarly journals Insight into the Structural Dynamics of the Lysenin During Prepore-to-Pore Transition Using Hydrogen–Deuterium Exchange Mass Spectrometry

Toxins ◽  
2019 ◽  
Vol 11 (8) ◽  
pp. 462 ◽  
Author(s):  
Magdalena Kulma ◽  
Michał Dadlez ◽  
Katarzyna Kwiatkowska
Keyword(s):  
Structural Dynamics ◽  
Pore Formation ◽  
Deuterium Exchange ◽  
Water Soluble ◽  
Soluble Form ◽  
Hydrogen Deuterium Exchange ◽  
Structural Stabilization ◽  
Terminal Domain ◽  
Hydrogen Deuterium ◽  
Β Sheet

Lysenin is a pore-forming toxin of the aerolysin family, which is derived from coelomic fluid of the earthworm Eisenia fetida. Upon binding to sphingomyelin (SM)-containing membranes, lysenin undergoes a series of structural changes promoting the conversion of water-soluble monomers into oligomers, leading to its insertion into the membrane and the formation of a lytic β-barrel pore. The soluble monomer and transmembrane pore structures were recently described, but the underlying structural details of oligomerization remain unclear. To investigate the molecular mechanisms controlling the conformational rearrangements accompanying pore formation, we compared the hydrogen–deuterium exchange pattern between lyseninWT and its mutant lyseninV88C/Y131C. This mutation arrests lysenin oligomers in the prepore state at the membrane surface and does not affect the structural dynamics of the water-soluble form of lysenin. In contrast, membrane-bound lyseninV88C/Y131C exhibited increased structural stabilization, especially within the twisted β-sheet of the N-terminal domain. We demonstrated that the structural stabilization of the lysenin prepore started at the site of lysenin’s initial interaction with the lipid membrane and was transmitted to the twisted β-sheet of the N-terminal domain, and that lyseninV88C/Y131C was arrested in this conformation. In lyseninWT, stabilization of these regions drove the conformational changes necessary for pore formation.

scholarly journals Patterns of structural dynamics in RACK1 protein retained throughout evolution: A hydrogen-deuterium exchange study of three orthologs

2014 ◽  
Vol 23 (5) ◽  
pp. 639-651 ◽  
Author(s):  
Krzysztof Tarnowski ◽  
Kinga Fituch ◽  
Roman H. Szczepanowski ◽  
Michal Dadlez ◽  
Magdalena Kaus-Drobek
Keyword(s):  
Structural Dynamics ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Exchange Study ◽  
Hydrogen Deuterium

Combining Ion Mobility Spectrometry with Hydrogen-Deuterium Exchange and Top-Down MS for Peptide Ion Structure Analysis

2014 ◽  
Vol 25 (12) ◽  
pp. 2103-2115 ◽  
Author(s):  
Mahdiar Khakinejad ◽  
Samaneh Ghassabi Kondalaji ◽  
Hossein Maleki ◽  
James R. Arndt ◽  
Gregory C. Donohoe ◽  
...  
Keyword(s):  
Structure Analysis ◽  
Ion Mobility Spectrometry ◽  
Ion Mobility ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Top Down ◽  
Ion Structure ◽  
Hydrogen Deuterium ◽  
Peptide Ion Structure

scholarly journals Structural Dynamics of 15-Lipoxygenase-2 via Hydrogen–Deuterium Exchange

Biochemistry ◽  
2017 ◽  
Vol 56 (38) ◽  
pp. 5065-5074 ◽  
Author(s):  
Kristin D. Droege ◽  
Mary E. Keithly ◽  
Charles R. Sanders ◽  
Richard N. Armstrong ◽  
Matthew K. Thompson
Keyword(s):  
Structural Dynamics ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Hydrogen Deuterium
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