scholarly journals Characterization of IgG1 Conformation and Conformational Dynamics by Hydrogen/Deuterium Exchange Mass Spectrometry

2009 ◽  
Vol 81 (7) ◽  
pp. 2644-2651 ◽  
Author(s):  
Damian Houde ◽  
Joseph Arndt ◽  
Wayne Domeier ◽  
Steven Berkowitz ◽  
John R. Engen
Keyword(s):  
Mass Spectrometry ◽  
Conformational Dynamics ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Exchange Mass Spectrometry ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry

scholarly journals Characterization of IgG1 Conformation and Conformational Dynamics by Hydrogen/Deuterium Exchange Mass Spectrometry

2009 ◽  
Vol 81 (14) ◽  
pp. 5966-5966 ◽  
Author(s):  
Damian Houde ◽  
Joseph Arndt ◽  
Wayne Domeier ◽  
Steven Berkowitz ◽  
John R. Engen
Keyword(s):  
Mass Spectrometry ◽  
Conformational Dynamics ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Exchange Mass Spectrometry ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry

scholarly journals Load-dependent destabilization of the γ-rotor shaft in FOF1 ATP synthase revealed by hydrogen/deuterium-exchange mass spectrometry

2016 ◽  
Vol 113 (9) ◽  
pp. 2412-2417 ◽  
Author(s):  
Siavash Vahidi ◽  
Yumin Bi ◽  
Stanley D. Dunn ◽  
Lars Konermann
Keyword(s):  
Mass Spectrometry ◽  
Molecular Motor ◽  
Conformational Dynamics ◽  
Bound State ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Exchange Mass Spectrometry ◽  
Hydrogen Deuterium ◽  
Membrane Bound ◽  
Deuterium Exchange Mass Spectrometry

FoF1 is a membrane-bound molecular motor that uses proton-motive force (PMF) to drive the synthesis of ATP from ADP and Pi. Reverse operation generates PMF via ATP hydrolysis. Catalysis in either direction involves rotation of the γε shaft that connects the α3β3 head and the membrane-anchored cn ring. X-ray crystallography and other techniques have provided insights into the structure and function of FoF1 subcomplexes. However, interrogating the conformational dynamics of intact membrane-bound FoF1 during rotational catalysis has proven to be difficult. Here, we use hydrogen/deuterium exchange mass spectrometry to probe the inner workings of FoF1 in its natural membrane-bound state. A pronounced destabilization of the γ C-terminal helix during hydrolysis-driven rotation was observed. This behavior is attributed to torsional stress in γ, arising from γ⋅⋅⋅α3β3 interactions that cause resistance during γ rotation within the apical bearing. Intriguingly, we find that destabilization of γ occurs only when FoF1 operates against a PMF-induced torque; the effect disappears when PMF is eliminated by an uncoupler. This behavior resembles the properties of automotive engines, where bearings inflict greater forces on the crankshaft when operated under load than during idling.

Ligand binding and conformational dynamics in a flavin-based electron-bifurcating enzyme complex revealed by Hydrogen-Deuterium Exchange Mass Spectrometry

FEBS Letters ◽  
2016 ◽  
Vol 590 (24) ◽  
pp. 4472-4479 ◽  
Author(s):  
Julius K. Demmer ◽  
Fiona A. Rupprecht ◽  
Martin L. Eisinger ◽  
Ulrich Ermler ◽  
Julian D. Langer
Keyword(s):  
Mass Spectrometry ◽  
Ligand Binding ◽  
Conformational Dynamics ◽  
Deuterium Exchange ◽  
Enzyme Complex ◽  
Hydrogen Deuterium Exchange ◽  
Exchange Mass Spectrometry ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry

Characterization of the N370S Mutant of Glucocerebrosidase by Hydrogen/Deuterium Exchange Mass Spectrometry

ChemBioChem ◽  
2012 ◽  
Vol 13 (15) ◽  
pp. 2243-2250 ◽  
Author(s):  
Liangjie Tang ◽  
Stephen J. Coales ◽  
Jeffrey A. Morrow ◽  
Tim Edmunds ◽  
Yoshitomo Hamuro
Keyword(s):  
Mass Spectrometry ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Exchange Mass Spectrometry ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry
Sign in / Sign up

Export Citation Format

Share Document