Publication: MCL-1 promiscuity and the structural resilience of its binding partners
MCL-1 promiscuity and the structural resilience of its binding partners
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Heckmeier, P. J., Ruf, J., Janković, B. G., & Hamm, P. (2023). MCL-1 promiscuity and the structural resilience of its binding partners. Journal of Chemical Physics, 158(9), 095101. https://doi.org/10.1063/5.0137239
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The allosteric protein MCL-1 and its natural inhibitors, the BH3-only proteins PUMA, BIM, and NOXA regulate apoptosis by interacting promiscuously within an entangled binding network. Little is known about the transient processes and dynamic conformational fluctuations that are the basis for the formation and stability of the MCL-1/BH3-only complex. In this study, we designed photoswitchable versions of MCL-1/PUMA and MCL-1/NOXA, and investigated the protein response after an ultrafast photo-perturbation with transient infrared spectr
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- Heckmeier, Philipp J
- Ruf, Jeannette
- Janković, Brankica G
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Heckmeier, P. J., Ruf, J., Janković, B. G., & Hamm, P. (2023). MCL-1 promiscuity and the structural resilience of its binding partners. Journal of Chemical Physics, 158(9), 095101. https://doi.org/10.1063/5.0137239
