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Updated: Apr 21, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Enzyme dynamics and engineering: one step at a time
Nobuhiko Tokuriki1, Colin J Jackson2
1Michael Smith Laboratories, University of British Columbia, Vancouver, BC V6T 1Z4, Canada.
Abstract:
Although protein dynamics are accepted as being essential for enzyme function, their effects are not fully understood. In this issue of Chemistry and Biology, Gobeil and coworkers describe how engineered changes in the millisecond motions of a mutant TEM-1 β-lactamase do not significantly affect substrate turnover. This mutational robustness has implications for protein engineering and design strategies.
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