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.
|Number of pages||6|
|Publication status||Published - 2018|
All Science Journal Classification (ASJC) codes
- Materials Science(all)
- Condensed Matter Physics
Levantino, M., Tidow, H., Niebling, S., Monteiro, D., Josts, I., Gao, Y., Gao, Y., & Levantino, M. (2018). Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization. IUCrJ, 5, 667-672.