An infrared laser-induced temperature jump provides a rapid and broadly applicable perturbation to protein dynamics. Temperature-jump crystallography was paired with time-resolved X-ray crystallography to study the dynamic enzyme lysozyme. Measurements with and without a functional inhibitor revealed different patterns in the propagation of motion throughout the enzyme.
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References
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This is a summary of: Wolff, A. M. et al. Mapping protein dynamics at high spatial resolution with temperature-jump X-ray crystallography. Nat. Chem. https://doi.org/10.1038/s41557-023-01329-4 (2023).
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Visualization of protein motions using temperature-jump crystallography. Nat. Chem. 15, 1497–1498 (2023). https://doi.org/10.1038/s41557-023-01331-w
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DOI: https://doi.org/10.1038/s41557-023-01331-w
