Full-length huntingtin protein aggregation and first attempts to co-purify HTT-HAP40 from insect cells

This past week, I have been completing experiments in two different threads:

1. I have used the different polyQ length huntingtin protein samples I made previously in an experiment which measures how the protein molecules aggregate (stick together) when heated. This technique is called differential static light scattering (DSLS). I saw no difference in the thermal aggregation properties of the samples and no correlation between these biophysical attributes and polyQ length.

DSLS analysis of HTT Q19, Q23, Q42 and Q54 showing similar thermal aggregation transition temperatures

2. To replicate the work of Gun et al (2018), I am reproducing the purification of the HTT-HAP40 complex. This experiment serves a number of purposes. Firstly to validate the insect cell expression system for HTT complex generation. Secondly to check my protocol for HTT-complex purification works. I think I have purified the complex but am scaling the production to make much more sample soon and need to run some additional checks. I will use this material to investigate HTT-HAP40 DNA binding too.

I also got some good news as I have been selected for the HDSA Berman Topper Fellowship award! I am incredibly thankful to have been chosen and excited to continue working on HTT!!

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