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

<strong>Project: </strong>Biophysical investigation of purified HTT protein samples

<strong>Experiment: </strong>A time-course analysis using Differential Static Light Scattering (DSLS) of purified HTT^1-3144Q23

<strong>Date completed:­ </strong>2019/01/28

<strong>Rationale: </strong>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.