Identification of three phases in Onconase refolding

• Published in: The FEBS journal Vol. 274; no. 22; pp. 5826 - 5833
• Main Authors: Schulenburg, Cindy, Martinez-Senac, Maria M, Löw, Christian, Golbik, Ralph, Ulbrich-Hofmann, Renate, Arnold, Ulrich
• Format: Journal Article
• Language: English
• Published: Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.11.2007; Blackwell Publishing Ltd
• Subjects: Biochemistry; Catalysis; intermediate; Kinetics; Models, Molecular; Molecular biology; Onconase; proline isomerization; Protein Folding; Protein Structure, Tertiary; reactivation; Ribonucleases - metabolism; Spectrometry, Fluorescence; Thermodynamics

Onconase is an extremely stable member of the RNase A superfamily. The increase in the thermodynamic stability by 20 kJ·mol⁻¹ in comparison to RNase A was expected to result in altered folding behavior. Despite the lack of cis-Pro residues in native Onconase, refolding at low concentrations of guani...