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Updated: Jul 25, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
Impact of protein flexibility on hydride-transfer parameters in thermophilic and psychrophilic alcohol dehydrogenases
Zhao-Xun Liang1, Iason Tsigos, Vassilis Bouriotis
1Departments of Chemistry and Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Abstract:
The hydride transfer catalyzed by thermophilic alcohol dehydrogenase (htADH) exhibits sharply different kinetic and activation parameters from that catalyzed by the more flexible psychrophilic alcohol dehydrogenase (psADH). In addition, the hydride transfer in htADH is affected by mutating two distal residues that are suggested to be responsible for the decreased local protein flexibility in htADH. These observations provide support for the view that protein dynamics is tightly coupled to the hydrogen-transfer processes in these enzymes.
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