What is it about?
Proteins change shape while performing their function. Some undergo small, local changes and others larger global changes. Watching these events in real time can be done using X-rays, but it is a challenging experiment as all the proteins in the sample have to be synchronised. We used a light-reactive molecule to synchronise the proteins and watched the proteins bind the small molecule and dimerise. Laser flashes are ideal for synchronisation but most proteins do not react to light. Nevertheless, many proteins, such as ours, react with small molecules that can be chemically modified to be light reactive.
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Why is it important?
Understanding protein motions allows us to understand protein function and mis-function. Being able to watch proteins carry out their jobs in real time can lead to the design of better medications and the engineering of more efficient proteins.
Perspectives
I believe this article will prompt serveral biochemistry/biophysics groups to think about this technique as a possible route to answer some of their complex questions. We have proven that the technique works in this pilot experiment. This work and this article were also a fantastic personal experience. The team was composed mainly by junior researchers belonging to different research groups. This publication showed a lot of collaboration and synergy between the different skill sets of everyone involved.
Diana Monteiro
Universitat Hamburg
Read the Original
This page is a summary of: Photocage-initiated time-resolved solution X-ray scattering investigation of protein dimerization, IUCrJ, September 2018, International Union of Crystallography,
DOI: 10.1107/s2052252518012149.
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