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PubMed · 9600927

Huntingtin aggregation monitored by dynamic light scattering.

Y Georgalis·E B Starikov·B Hollenbach·R Lurz·E Scherzinger·W Saenger·H Lehrach·E E Wanker
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Abstract

An initial stage of fibrillogenesis in solutions of glutathione S-transferase-huntingtin (GST-HD) fusion proteins has been studied by using dynamic light scattering. Two GST-HD systems with poly-L-glutamine (polyGln) extensions of different lengths (20 and 51 residues) have been examined. For both systems, kinetics of z-average translation diffusion coefficients (Dapp) and their angular dependence have been obtained. Our data reveal that aggregation does occur in both GST-HD51 and GST-HD20 solutions, but that it is much more pronounced in the former. Thus, our approach provides a powerful tool for the quantitative assay of GST-HD fibrillogenesis in vitro.

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Glutathione TransferaseHumansHuntingtin ProteinHuntington DiseaseLightNerve Tissue ProteinsNuclear ProteinsProtein ConformationRecombinant Fusion ProteinsSpectrum AnalysisJournal ArticleResearch Support, Non-U.S. Gov't

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Y Georgalis, E B Starikov, B Hollenbach, R Lurz, E Scherzinger, W Saenger, H Lehrach, E E Wanker. 1998-05-26. Huntingtin aggregation monitored by dynamic light scattering.. https://doi.org/10.1073/pnas.95.11.6118

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