Millisecond Hydrogen Exchange

Chemistry Department and Center for Re search in Mass Spectrometry, York University, Toronto, Ontario, Canada 

Hydrogen Exchange Mass Spectrometry of Proteins Fundamentals, Methods, and Applications, First Edition. Edited by David D. Weis. 

The first millisecond protein HX measurements were made by automated quench-flow pulse labeling and were aimed at characterizing early protein-folding intermediates [15, 16]. In these experiments, unlabeled protein was mixed with D O and incubated for a short period (ms), followed by a rapid pH drop and flash freeze to quench the reaction. Labeled samples were then analyzed by NMR (this was 1988, the same year that John Fenn showed the first electrospray protein mass spectra at the American Society for Mass Spectrometry meeting). Quench-flow HX for protein folding was translated to MS a few years later by Miranker and coworkers [17]. 

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Millisecond Hydrogen Exchange 87 5.4.5 Residual Structure in Intrinsically Disordered Proteins... 

Detection of Residual Helicity in ACTR with Millisecond Hydrogen Exchange... 

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