Journal
JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
Volume 32, Issue 7, Pages 1610-1617Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jasms.0c00475
Keywords
hydrogen exchange; mass spectrometry; statistical analysis; experimental error; uncertainty propagation; HX-MS
Funding
- National Science Foundation [CHE-1709176]
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Hydrogen exchange-mass spectrometry (HX-MS) is widely used to characterize higher-order protein structure and identify changes in protein structure and dynamics. This study applies uncertainty propagation principles to differential HX measurements and shows that pooled estimates of experimental uncertainty result in a lower false positive rate.
Hydrogen exchange-mass spectrometry (HX-MS) is used widely to characterize higher-order protein structure and to locate changes in protein structure and dynamics that accompany, for example, ligand binding and protein-protein interactions. Quantitative differences in the amount of hydrogen exchange between two states (i.e., differential HX) are taken as evidence of significant differences in higher-order structure or dynamics. The quantitative measures range from simple mass differences at one HX labeling time to differences averaged across an HX time course with correction for deuterium recovery. This work applies the principles of uncertainty propagation to differential HX measurements to facilitate the identification of significant differences. Furthermore, it is shown that pooled estimates of experimental uncertainty result in a lower false positive rate than estimates of uncertainty based on individual standard deviations.
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