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3 results for “Differential static light scattering”
Differential static light scattering (DSLS) of full-length huntingtin samples of different polyQ lengths (Q19, Q23, Q42 and Q54) – 2018/05/09
<p><strong>Project</strong> - Huntingtin structure-function open lab notebook. </p> <p><strong>Experiment</strong> - Differential static light scattering (DSLS) of full-length huntingtin samples of different polyQ lengths (Q19, Q23, Q42 and Q54) – 2018/05/09. To investigate how increased polyQ length of the huntingtin protein affects its biophysical properties. </p> <p> </p>
A time-course analysis using Differential Static Light Scattering (DSLS) of purified HTT1-3144 Q23 - 2019/01/28
<p><strong>Project: </strong>Biophysical investigation of purified HTT protein samples</p> <p><strong>Experiment: </strong>A time-course analysis using Differential Static Light Scattering (DSLS) of purified HTT<sup>1-3144</sup>Q23 </p> <p><strong>Date completed:­ </strong>2019/01/28</p> <p><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. </p>
Differential static light scattering (DSLS) of huntingtin-HAP40 complex samples of different polyQ lengths (Q23 and Q54) – 2018/10/13
<p>Project - Huntingtin structure-function open lab notebook. </p> <p>Experiment - Differential static light scattering (DSLS) of huntingtin-HAP40 complex samples of different polyQ lengths (Q23 and Q54) - 2018/10/13. To investigate how increased polyQ length of the huntingtin protein and complex formation of HAP40 might affect thermal aggregation properties of the samples. </p>
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