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.
Original language | English |
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Pages (from-to) | 1259-1260 |
Number of pages | 2 |
Journal | Chemistry and Biology |
Volume | 21 |
Issue number | 10 |
DOIs | |
Publication status | Published - 23 Oct 2014 |