Anion Shielding of Electrostatic Repulsions in Transthyretin Modulates Stability and Amyloidosis: Insight into the Chaotrope Unfolding Dichotomy

The balance between stabilizing forces and the localized electrostatic repulsions destabilizing the transthyretin (TTR) tetramer is tunable via anion shielding. The two symmetrical anion interaction sites in TTR are comprised of residues Lys15 and Lys15‘ from opposing subunits on the periphery of th...

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Veröffentlicht in:	Biochemistry (Easton) 2001-09, Vol.40 (38), p.11453-11459
Hauptverfasser:	Hammarström, Per, Jiang, Xin, Deechongkit, Songpon, Kelly, Jeffery W
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Amyloid - metabolism Amyloidosis - metabolism Anions Binding Sites Cross-Linking Reagents Drug Stability Glutaral Guanidine Humans Kinetics Macromolecular Substances Models, Molecular Mutagenesis, Site-Directed Potassium Chloride Prealbumin - chemistry Prealbumin - metabolism Protein Conformation Protein Denaturation Protein Folding Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Static Electricity Thyroxine - metabolism Urea
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