Article
Altered ionization of the B13 Glu in insulin B9 and B10 mutants: a computational analysis.
Protein engineering, design & selection : PEDS - 1 Jul 2004
Greaves Richard B, Dodson Guy G, Verma Chandra S
Abstract excerpt
An experimentally determined pK(a) change of +2.50 units has been reported for the B13 Glu residue in a dimeric B9 Ser --> Asp insulin mutant relative to the native dimer. Poisson-Boltzmann electrostatics-based pK(a) calculations were performed to probe the effect of the B9 Ser --> Asp and B10 His --> Asp mutations on aggregation and the ionization behaviour of the B13 carboxylate. The method produced shifts of...
Topics
- Amino Acid Sequence
- Animals
- Binding Sites
- Crystallography, X-Ray
- Dimerization
- Glutamic Acid
- Hydrogen-Ion Concentration
- Insulin
- Ions
- Kinetics
- Models, Molecular
- Models, Theoretical
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Software