Validating huntingtin domain protein samples

Last week I did some experiments to check that the protein samples I made 1) are what I think they are i.e. not a contaminant in the sample and 2) are good quality protein – all data on Zenodo.

The protein is definitely the right amino acid sequence and it is not contaminated – wahey! However, it is not very stable so this requires more work to optimise the purification conditions of the sample. This also likely explains why I have had problems previously with sample reproducibility previously as there is a very fine temperature window in which the protein is stable.

Mass spectrum of the sample shows only one peak of the expected size

Hopefully I will be able to find a condition which stabilises my sample soon so I can move on to do some structural studies – if I want to try and crystallise my protein sample to try and solve the structure by X-ray crystallography, long-term stability will be important.

Onwards and upwards!

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