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
van den Bedem, H. & Fraser, J. S. Integrative, dynamic structural biology at atomic resolution—it’s about time. Nat. Methods 12, 307–318 (2015). A review outlining a broad variety of approaches to studying protein dynamics.
Schmidt, M. Time-resolved macromolecular crystallography at modern X-ray sources. Methods Mol. Biol. 1607, 273–294 (2017). A review highlighting challenges and developments in methods for time-resolved crystallography.
Gruebele, M., Sabelko, J., Ballew, R. & Ervin, J. Laser temperature jump induced protein refolding. Acc. Chem. Res. 31, 699–707 (1998). A review covering infrared-induced temperature jumps coupled with spectroscopy to study proteins.
Keedy, D. A. et al. Mapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography. eLife 4, e07574 (2015). This paper reveals the effects of temperature on protein structures at thermal equilibrium.
Thompson, M. C. et al. Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme. Nat. Chem. 11, 1058–1066 (2019). This paper reports the use of temperature-jump paired with solution X-ray scattering to gain insight into functional protein dynamics.
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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
