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Christina has published her first research article in the Journal of the American Chemistry Society entitled “Ion Mobility Mass Spectrometry Unveils Global Protein Conformations in Response to Conditions that Promote and Reverse Liquid–Liquid Phase Separation.” This work was part of an ongoing collaboration with the Castañeda lab at Syracuse University in New York, as well as Christina’s industrial supervisor, Jakub Ujma from Waters Corp.

This project was to explore how the conformations of a disordered protein changes in response to solution conditions and how this can be measured using ion mobility mass spectrometry. The protein in question, UBQLN2, can form protein droplets in cells which are thought to mediate protein degradation pathways and when dysregulated, results in protein aggregates found in neurological diseases such as ALS. Thus, it is important to understand how the protein conformations can change and lead to these disease states.

In this article, we have shown that ion mobility mass spectrometry is an excellent analytical tool for probing the sutble yet important conformational changes that UBQLN2 undergoes when it forms protein droplets and when the droplets are dissolved by interacting with ubiquitin, a binding partner involved in the protein degradation pathway. We show that the protein becomes more elongated when droplet formation is promoted and that the complexes formed when ubiquitin is present are overall more compact than UBQLN2 alone.

The link to the full article can be seen below.

https://pubs.acs.org/doi/full/10.1021/jacs.3c00756

 

 

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