Article
Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.
Biophysical journal - 4 Apr 2012
Bradley John, O'Meara Fergal, Farrell Damien, Nielsen Jens Erik
Abstract excerpt
The majority of pK(a) values in protein unfolded states are close to the amino acid model pK(a) values, thus reflecting the weak intramolecular interactions present in the unfolded ensemble of most proteins. We have carried out thermal denaturation measurements on the WT and eight mutants of HEWL from pH 1.5 to pH 11.0 to examine the unfolded state pK(a) values and the pH dependence of protein stability for this...
Topics
- Animals
- Chemical Phenomena
- Hydrogen-Ion Concentration
- Molecular Dynamics Simulation
- Muramidase
- Mutagenesis, Site-Directed
- Mutation
- Protein Denaturation
- Protein Stability
- Temperature