Crowding agents and osmolytes provide insight into the formation and dissociation of RNase A oligomers

► Dextran and Ficoll increase the yields of RNase A oligomers. ► Stabilizing osmolytes slow RNase A oligomer dissociation. ► Rupture of intersubunit H-bonds is key for C-dimer dissociation. RNase A forms 3D domain-swapped oligomers with novel enzymatic and biological activities. We study how crowdin...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2011-02, Vol.506 (2), p.123-129
Hauptverfasser:	Ercole, Carmine, López-Alonso, Jorge Pedro, Font, Josep, Ribó, Marc, Vilanova, Maria, Picone, Delia, Laurents, Douglas V.
Format:	Artikel
Sprache:	eng
Schlagworte:	3D domain swapping Amyloid Animals bioactive properties Cattle Crowding deuterium Dextran Dextrans Dimerization dissociation Enzyme Stability Ficoll Glycine Hydrogen Hydrogen Bonding Hydrogen/deuterium exchange In Vitro Techniques Macromolecular crowding Methylamines Models, Molecular NMR spectroscopy Nuclear Magnetic Resonance, Biomolecular oxides Protein folding Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Protein Subunits ribonuclease A Ribonuclease, Pancreatic - chemistry ribonucleases Rupture sodium sulfate stabilizers
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