Protein: Thioredoxin 1 (Escherichia coli (strain K12))
UniProt: P0AA25
Mutation: D11E
PDB: 2TRX|2H6X
Experiment dataset: ProTherm
Method: Urea
Measure: fluorescence
pH: 7
Buffer: Hepes 5 mM
Temperature: 25
ddG: 5.7
Cm: 5.83
m-value: 1.22
Reversibility: no
State: 2.0
Reference: Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. — Godoy-Ruiz Raquel|Sanchez-Ruiz Jose M|Ariza Fernando|Rodriguez-Larrea David|Perez-Jimenez Raul|Ibarra-Molero Beatriz (J Mol Biol;362;966-78, 2006)