I work on Hv
I am currently working on the human voltage-gated proton channel Hv1. My main goal is to solve the structure of this protein by any means necessary.
The first approach has been to try and get crystals of the protein to use in diffraction experiments. This has proven to be extremely difficult! Let me just say that after working on this problem for two years I managed to get crystals that diffracted to moderate resolution and was able to solve a structure! However, it turned out that the protein was is a non-native partially unfolded state and therefore we were not able to learn anything about its proper structure or how the protein works. Science is hard! But I haven’t given up.
The structure of Hv would be a major break through. I will certainly be elaborating more in this blog about why Hv is important and why I feel proud to be dedicating my time and effort into advancing our understanding of this molecule.
To learn more about me and my work check out the My Work page or my ResearchGate profile.
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[…] work on a voltage-gated protein (Hv) and I have spent some time thinking about and studying the mechanism of how these voltage sensors […]
LettsScience 
Just a comment from a novice but is it possible to spike with a chaperone and allow physio conditioning before crystal growth, considerable task you are taking on by the way.
Hello Gerry,
Thanks for the comments. I have tried and am trying various chaperone strategies. I can’t say too much because it is still a work in progress. I am not sure exactly what you mean by physio conditioning. There was a time when I thought this task would be straight forward, we have a high resolution structure of the isolated voltage-sensor domain of KvAP right? How hard could the voltage-sensor-only protein be to crystallize? I have learn a lot since then…
However, if I thought it was hopeless I wouldn’t keep trying. Thanks again.
James