Is There Hydrogen Scrambling in the Gas Phase? Energetic and Structural Determinants of Proton Mobility within Protein Ions

2004 ◽  
Vol 126 (24) ◽  
pp. 7709-7717 ◽  
Author(s):  
Joshua K. Hoerner ◽  
Hui Xiao ◽  
Andras Dobo ◽  
Igor A. Kaltashov
Keyword(s):  
Gas Phase ◽  
Structural Determinants ◽  
Proton Mobility ◽  
Protein Ions ◽  
Hydrogen Scrambling

Visible and ultraviolet spectroscopy of gas phase protein ions

2011 ◽  
Vol 13 (37) ◽  
pp. 16494 ◽  
Author(s):  
Rodolphe Antoine ◽  
Philippe Dugourd
Keyword(s):  
Gas Phase ◽  
Ultraviolet Spectroscopy ◽  
Protein Ions ◽  
Phase Protein

scholarly journals Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Traveling Wave Device

2019 ◽  
Vol 91 (12) ◽  
pp. 7554-7561 ◽  
Author(s):  
Charles Eldrid ◽  
Jakub Ujma ◽  
Symeon Kalfas ◽  
Nick Tomczyk ◽  
Kevin Giles ◽  
...  
Keyword(s):  
Gas Phase ◽  
Ion Mobility Spectrometry ◽  
Phase Stability ◽  
Ion Mobility ◽  
Traveling Wave ◽  
Protein Ions ◽  
Wave Device

Do electrospray mass spectra reflect the ligand binding state of proteins in solution?

2005 ◽  
Vol 83 (11) ◽  
pp. 1953-1960 ◽  
Author(s):  
Belal M Hossain ◽  
Douglas A Simmons ◽  
Lars Konermann
Keyword(s):  
Mass Spectrometry ◽  
Gas Phase ◽  
Protein Interactions ◽  
Noncovalent Complex ◽  
Deuterium Exchange ◽  
Solution Phase ◽  
Hydrogen Deuterium Exchange ◽  
Esi Ms ◽  
Protein Ions ◽  
Hydrogen Deuterium

Electrospray ionization (ESI) mass spectrometry (MS) has become a popular tool for monitoring ligand–protein and protein–protein interactions. Due to the "gentle" nature of the ionization process, it is often possible to transfer weakly bound complexes into the gas phase, thus making them amenable to MS detection. One problem with this technique is the potential occurrence of fragmentation events during ESI. Also, some analytes tend to cluster together during ionization, thus forming nonspecific gas-phase assemblies that do not represent solution-phase complexes. In this work, we implemented a hydrogen–deuterium exchange (HDX) approach that can reveal whether or not the free and (or) bound constituents of a complex observed in ESI-MS reflect the binding situation in solution. Proteins are subjected to ESI immediately following an isotopic labeling pulse; only ligand-free and ligand-bound protein ions that were formed directly from the corresponding solution-phase species showed different HDX levels. Using myoglobin as a model system, it is demonstrated that this approach can readily distinguish scenarios where the heme–protein interactions were disrupted in solution from those where dissociation of the complex occurred in the gas phase. Experiments on cytochrome c strongly suggest that dimeric protein ions observed in ESI-MS reflect aggregates that were formed in solution.Key words: electrospray mass spectrometry, ligand–protein interaction, noncovalent complex, hydrogen–deuterium exchange, protein folding.

scholarly journals Effects of Metal Ion Adduction on the Gas-Phase Conformations of Protein Ions

2013 ◽  
Vol 24 (11) ◽  
pp. 1654-1662 ◽  
Author(s):  
Tawnya G. Flick ◽  
Samuel I. Merenbloom ◽  
Evan R. Williams
Keyword(s):  
Gas Phase ◽  
Metal Ion ◽  
Protein Ions ◽  
Metal Ion Adduction

scholarly journals On the Zwitterionic Nature of Gas-Phase Peptides and Protein Ions

2010 ◽  
Vol 6 (5) ◽  
pp. e1000775 ◽  
Author(s):  
Roberto Marchese ◽  
Rita Grandori ◽  
Paolo Carloni ◽  
Simone Raugei
Keyword(s):  
Gas Phase ◽  
Protein Ions

scholarly journals Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Travelling Wave Device

2018 ◽  
Author(s):  
Charles Eldrid ◽  
Jakub Ujma ◽  
Symeon Kalfas ◽  
nick tomczyk ◽  
Kevin Giles ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Gas Phase ◽  
Ion Mobility ◽  
Structural Changes ◽  
Structural Information ◽  
Travelling Wave ◽  
Resolving Power ◽  
Small Proteins ◽  
Multimeric Complex ◽  
Protein Ions

<div>Ion mobility mass spectrometry (IM-MS) allows separation of native protein ions into “conformational families”. Increasing the IM resolving power should allow finer structural information to be obtained, and can be achieved by increasing the length of the IM separator. This, however, increases the time that protein ions spend in the gas phase and previous experiments have shown that the initial conformations of small proteins can be lost within tens of milliseconds. Here, we report on investigations of protein ion stability using a multi-pass travelling wave (TW) cyclic IM (cIM) device. Using this device, minimal structural changes were observed for Cytochrome C after hundreds of milliseconds, while no changes were observed for a larger multimeric complex (Concanavalin A). The geometry of the instrument (Q-cIM-ToF) also enables complex tandem IM experiments to be performed which were used to obtain more detailed collision induced unfolding pathways for Cytochrome C. The novel instrument geometry provide unique capabilities with the potential to expand the field of protein analysis via IM-MS.</div>

Sign in / Sign up

Export Citation Format

Share Document