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- W2087225658 abstract "In recent years, the application of pressure on biological systems has gained increasing interest. Pressure-induced destabilization of electrostatic and hydrophobic interactions is currently exploited to study conformational protein stability and macromolecular assemblies of proteins. Due to links between severe human pathologies and ordered protein oligomerization into aggregates, which have become apparent, a better knowledge of the molecular and structural determinants that ensure the packing efficiency and stability of such complexes has taken on special importance. Here, we report the effect of pressure on the property of human ataxin-3 of aggregation. The results indicate the importance of its polyglutamine chain length in the stability and the tendency of the protein to form spheroids. Partial unfolding of the protein leading to solvent exposure of hydrophobic domains appears to be a prerequisite in the aggregation process of ataxin-3." @default.
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- W2087225658 date "2004-03-26" @default.
- W2087225658 modified "2023-10-16" @default.
- W2087225658 title "High pressure as a tool for investigating protein–ligand interactions" @default.
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- W2087225658 doi "https://doi.org/10.1088/0953-8984/16/14/039" @default.
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