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.

Marchal, S., Lange, R., Tortora, P., Balny, C. (2004). High pressure as a tool for investigating protein-ligand interactions. JOURNAL OF PHYSICS. CONDENSED MATTER, 16(14), S1271-S1275 [10.1088/0953-8984/16/14/039].

High pressure as a tool for investigating protein-ligand interactions

TORTORA, PAOLO;
2004

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.
Articolo in rivista - Articolo scientifico
hig pressure; protein stability; protein aggregation; protein-ligand interaction
English
14-apr-2004
16
14
S1271
S1275
none
Marchal, S., Lange, R., Tortora, P., Balny, C. (2004). High pressure as a tool for investigating protein-ligand interactions. JOURNAL OF PHYSICS. CONDENSED MATTER, 16(14), S1271-S1275 [10.1088/0953-8984/16/14/039].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/27437
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