Article
The mutation K30D disrupts the only salt bridge at the subunit interface of the homodimeric hemoglobin from Scapharca inaequivalvis and changes the mechanism of cooperativity.
The Journal of biological chemistry - 1 Mar 2002
Ceci Pierpaolo, Giangiacomo Laura, Boffi Alberto, Chiancone Emilia
Abstract excerpt
The subunit interface of the homodimeric hemoglobin from Scapharca inaequivalvis, HbI, is stabilized by a network of interactions that involve several hydrogen-bonded structural water molecules, a hydrophobic patch, and a single, symmetrical salt bridge between residues Lys-30 and Asp-89. Upon mutation of Lys-30 to Asp, the interface is destabilized markedly. Sedimentation equilibrium and velocity experiments...
Topics
- Animals
- Dimerization
- Dose-Response Relationship, Drug
- Escherichia coli
- Heme
- Hemoglobins
- Hydrogen
- Hydrogen-Ion Concentration
- Kinetics
- Ligands
- Lysine
- Mollusca
- Mutagenesis, Site-Directed
- Mutation