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Journal Article

Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization


Gao,  Y.
The Department of Chemistry, The University of Hamburg;
International Max Planck Research School for Ultrafast Imaging & Structural Dynamics (IMPRS-UFAST), Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;

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Josts, I., Niebling, S., Gao, Y., Levantino, M., Tidowa, H., & Monteiroa, D. (2018). Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization. IUCrJ, 5(6), 667-672. doi:10.1107/S2052252518012149.

Cite as: https://hdl.handle.net/21.11116/0000-0002-7F79-9
This work demonstrates a new method for investigating time-resolved structural changes in protein conformation and oligomerization via photocage-initiated time-resolved X-ray solution scattering by observing the ATP-driven dimerization of the MsbA nucleotide-binding domain. Photocaged small molecules allow the observation of single-turnover reactions of non-naturally photoactivatable proteins. The kinetics of the reaction can be derived from changes in X-ray scattering associated with ATP-binding and subsequent dimerization. This method can be expanded to any small-molecule-driven protein reaction with conformational changes traceable by X-ray scattering where the small molecule can be photocaged.