2017
DOI: 10.3791/55464-v
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Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics

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Cited by 3 publications
(2 citation statements)
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“…Proteins undergo the H/D exchange during the electrophoresis while migrating in the capillary in the deuterated background electrolyte solution, and this is followed by top-down MS analysis and gas-phase fragmentations to assess the deuterium uptake levels at both the global and fragment levels. Lastly, there are also two other methods in this collection that highlight different methods of H/D exchange, namely exchange for lyophilized power 8 and exchange after electrospray ionization 9 .…”
Section: Ms-based Protein Footprinting Approaches Assess Thementioning
confidence: 99%
“…Proteins undergo the H/D exchange during the electrophoresis while migrating in the capillary in the deuterated background electrolyte solution, and this is followed by top-down MS analysis and gas-phase fragmentations to assess the deuterium uptake levels at both the global and fragment levels. Lastly, there are also two other methods in this collection that highlight different methods of H/D exchange, namely exchange for lyophilized power 8 and exchange after electrospray ionization 9 .…”
Section: Ms-based Protein Footprinting Approaches Assess Thementioning
confidence: 99%
“…In higher-order conformations, more structured and solvent inaccessible regions are protected from exchange compared to disordered and solvent accessible regions of the molecule [5]. The m/z shifts arising from isotopic exchange within the latter regions are currently exploited by HDX-MS to study structures of challenging systems [18][19][20][21][22][23][24][25][26] folding dynamics [27][28][29][30][31], protein-protein and protein-oligonucleotide interactions [32][33][34][35][36][37][38][39][40], as well as protein-ligand interactions and any associated conformational changes [41][42][43][44][45][46][47][48][49].…”
Section: Introductionmentioning
confidence: 99%