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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Glutathione Transferase / chemistry*
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Glutathione Transferase / genetics
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Glutathione Transferase / metabolism
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Humans
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Huntingtin Protein
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Huntington Disease / metabolism*
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Light
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / genetics
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Nerve Tissue Proteins / metabolism
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Nuclear Proteins / chemistry*
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism
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Protein Conformation*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Spectrum Analysis
Substances
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HTT protein, human
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Huntingtin Protein
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Nerve Tissue Proteins
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Nuclear Proteins
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Recombinant Fusion Proteins
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Glutathione Transferase