scholarly journals Kinetics of gas-phase hydrogen/deuterium exchange and gas-phase structure of protonated phenylalanine, proline, tyrosine and tryptophan

2003 ◽  
Vol 17 (24) ◽  
pp. 2769-2772 ◽  
Author(s):  
Marko Ro?man ◽  
Sa?a Kazazi? ◽  
Leo Klasinc ◽  
Dunja Srzi?
Keyword(s):  
Gas Phase ◽  
Phase Structure ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Hydrogen Deuterium ◽  
Gas Phase Structure ◽  
Kinetics Of

Hydrogen-deuterium exchange reactions of carbanions with deuterated alcohols in the gas phase

1978 ◽  
Vol 100 (9) ◽  
pp. 2921-2922 ◽  
Author(s):  
C. H. DePuy ◽  
Veronica M. Bierbaum ◽  
Gary K. King ◽  
R. H. Shapiro
Keyword(s):  
Gas Phase ◽  
Deuterium Exchange ◽  
Hydrogen Deuterium Exchange ◽  
Exchange Reactions ◽  
Hydrogen Deuterium

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.

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