Chemistry Publications
Document Type
Article
Publication Date
10-26-2021
Journal
Analytical chemistry
Volume
93
Issue
42
First Page
14121
Last Page
14129
URL with Digital Object Identifier
https://doi.org/10.1021/acs.analchem.1c02471
Abstract
Many aspects of protein function rely on conformational fluctuations. Hydrogen/deuterium exchange (HDX) mass spectrometry (MS) provides a window into these dynamics. Despite the widespread use of HDX-MS, it remains unclear whether this technique provides a truly comprehensive view of protein dynamics. HDX is mediated by H-bond-opening/closing events, implying that HDX methods provide an H-bond-centric view. This raises the question if there could be fluctuations that leave the H-bond network unaffected, thereby rendering them undetectable by HDX-MS. We explore this issue in experiments on cytochrome
