Protein: Subtilisin-chymotrypsin inhibitor-2A (Hordeum vulgare)
UniProt: P01053
Mutation: K22A|E27A
PDB: 2CI2
Experiment dataset: ProTherm
Method: GdnHCl
Measure: Fluorescence
pH: 6.25
Buffer: MES 50 mM
Temperature: 25
dG: 6.43
ddG: 1.17
Cm: 3.43
m-value: 1.87
Reversibility: yes
Reference: The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. — Fersht A R|Otzen D E|Itzhaki L S (J Mol Biol;254;260-88, 1995)