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A time-course analysis using Differential Static Light Scattering (DSLS) of purified HTT1-3144 Q23 - 2019/01/28

dataset
posted on 28.01.2019, 00:00 by Harding, Rachel, Arrowsmith, Cheryl, Lee, Matt

Project: Biophysical investigation of purified HTT protein samples

Experiment: A time-course analysis using Differential Static Light Scattering (DSLS) of purified HTT1-3144Q23 

Date completed:­ 2019/01/28

Rationale: Time and resources in the HD field have been primarily focussed on understanding HTT aggregation looking as caspase cleavage products spanning aa. 1-586 or exon 1 spanning aa. 1-90. However, we know that HTT protein purified in its apo form is able to self-associate into larger oligomeric species and that monomer, dimer and larger species are found following FLAG-affinity chromatography as determined by size-exclusion chromatography (SEC) and SEC-multi-angle light scattering (SEC-MALS). This experiment aimed to begin to investigate how HTT self-associates and aggregates over time in a range of different conditions. 

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