Hydrogen exchange (HX) is an innovative technique used to examine protein conformation and dynamics while being monitored by mass spectrometry (MS). The method is used to observe the exchange of hydrogen atoms of protein backbone amides for deuterium atoms. To induce the exchange, a protein is exposed to D<sub>2</sub>O on a time interval. During that time, hydrogen atoms are exchanged for deuterium atoms, however, the technique cannot measure individual amides because the HX-MS method only measures at a peptide level. This study investigates whether the HX-MS techniques agrees with the HX-NMR technique through residue level calculations and HX-MS peptide level calculations. Ubiquitin was used as a model protein for the study. The results obtained from the HX-NMR gives residue level protection factors. HX-NMR residue level measurements obtained from a previous experiment were used to predict the peptide level measurements for the HX-MS method. From the study conducted the results revealed that there was some agreement between some peptides from both HX methods while there were some peptides that were not in agreement.<br/><br/>

Testing agreements between NMR and mass spectrometry HX method

253rd National Meeting (2017)

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