Publication: The Speed of Allosteric Signaling Within a Single-Domain Protein
The Speed of Allosteric Signaling Within a Single-Domain Protein
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Božović, O., Ruf, J., Zanobini, C., Jankovic, B., Buhrke, D., Johnson, P. J. M., & Hamm, P. (2021). The Speed of Allosteric Signaling Within a Single-Domain Protein. Journal of Physical Chemistry Letters, 12(17), 4262–4267. https://doi.org/10.1021/acs.jpclett.1c00915
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While much is known about different allosteric regulation mechanisms, the nature of the allosteric signal and the time scale on which it propagates remains elusive. The PDZ3 domain from postsynaptic density-95 protein is a small protein domain with a terminal third α-helix, i.e., the α3-helix, which is known to be allosterically active. By cross-linking the allosteric helix with an azobenzene moiety, we obtained a photocontrollable PDZ3 variant. Photoswitching triggers its allosteric transition, resulting in a change in binding affini
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Božović, O., Ruf, J., Zanobini, C., Jankovic, B., Buhrke, D., Johnson, P. J. M., & Hamm, P. (2021). The Speed of Allosteric Signaling Within a Single-Domain Protein. Journal of Physical Chemistry Letters, 12(17), 4262–4267. https://doi.org/10.1021/acs.jpclett.1c00915