A strategy using pressure was devised to structurally identify conformational transitions in protein ensembles, allowing the rational prediction of mutations that induce pressure-driven enzyme activation. These results highlight the power of flexibility–function analyses in protein engineering design and applications.
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References
Campbell, E. et al. Nat. Chem. Biol. 12, 944–50 (2016).
Narayanan, C. et al. Structure 26, 426–36 (2018).
Stiller, J. B. et al. Nat. Catal. https://doi.org/10.1038/s41929-019-0307-6 (2019).
Lisi, G. P. & Loria, J. P. Prog. Nucl. Magn. Reson. Spectrosc. 92–93, 1–17 (2016).
Akasaka, K. Chem. Rev. 106, 1814–35 (2006).
Wilding, M., Hong, N., Spence, M., Buckle, A. M. & Jackson, C. J. Biochem. Soc. Trans. 47, 701–11 (2019).
Davey, J. A., Damry, A. M., Goto, N. K. & Chica, R. A. Nat. Chem. Biol. 13, 1280–85 (2017).
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Doucet, N. Enzyme catalysis under pressure. Nat Catal 2, 646–647 (2019). https://doi.org/10.1038/s41929-019-0326-3
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DOI: https://doi.org/10.1038/s41929-019-0326-3
