Huntingtin aggregation monitored by dynamic light scattering.
basic_science · Level V
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- Record sourced from PubMed, PMID 9600927.
- Also identified by PMC identifier 27595.
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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.
Medical subject headings
- Glutathione Transferase
- Huntington Disease
- Nerve Tissue Proteins
- Nuclear Proteins
- Protein Conformation