Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation

By Zhongqi Zhang, David L. Smith. 1993

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1. Lemin Zheng
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5. B. Pascal
6. M. Brennan
7. D. Weis
8. Mingjiang Sun

Citations in the corpus

• Analysis of Overlapped and Noisy Hydrogen/Deuterium Exchange Mass Spectra (2013, background): “Since the earliest experiments, it has been realized that uncorrelated local dynamics yield a binomial exchange profile (EX2 regime) whereas more global correlated unfolding events result in a bimodal exchange pattern (EX1 regime) [13].”
• Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease. (2004, methodology): “The hydrogen/deuterium exchange method is based on monitoring the ability of backbone amide protons to exchange with the solvent as a measure of solvent accessibility — a process that occurs readily at neutral pH, but that can be slowed 10 orders of magnitude at acidic pH (pH 2) (39, 40).”
• Transcriptome engineering with RNA-targeting Type VI-D CRISPR effectors (2018, unknown): “This is accomplished determining the observed averages of the undeuterated and fully deuterated spectra and using the conventional formula described elsewhere (Zhang and Smith, 1993).”
• HDX Workbench: Software for the Analysis of H/D Exchange MS Data (2012, methodology): “The second ‘centroid’ method is achieved by calculating the weighted average of all spectral data within defined m/z limits, and determining %D by comparing the result to defined minimum and maximum m/z values [32].”
• Mapping Residual Structure in Intrinsically Disordered Proteins at Residue Resolution Using Millisecond Hydrogen/Deuterium Exchange and Residue Averaging (2015, methodology): “Data were normalized to 100% relative to a totally deuterated control [15].”