| Literature DB >> 9600927 |
Y Georgalis1, E B Starikov, B Hollenbach, R Lurz, E Scherzinger, W Saenger, H Lehrach, E E Wanker.
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.Entities:
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Year: 1998 PMID: 9600927 PMCID: PMC27595 DOI: 10.1073/pnas.95.11.6118
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205