Article
Thermodynamic studies on the equilibrium properties of a series of recombinant betaW37 hemoglobin mutants.
Biochemistry - 31 Mar 1998
Kiger L, Klinger A L, Kwiatkowski L D, De Young A, Doyle M L, Holt J M, Noble R W, Ackers G K
Abstract excerpt
In human hemoglobin (Hb) the beta37 tryptophan residue (betaW37), located at the hinge region of the alpha1beta2 interface, forms many contacts with alpha subunit residues of the opposite dimer, in both the T and R quaternary structures. We have carried out equilibrium O2 binding studies on a series of recombinant Hbs that have mutations at this residue site: betaW37Y, betaW37A, betaW37G, and betaW37E. Binding...
Topics
- Amino Acid Substitution
- Chromatography, Gel
- Cross-Linking Reagents
- Hemoglobin A
- Humans
- Mutation
- Oxygen
- Phytic Acid
- Protein Binding
- Protein Conformation
- Recombinant Proteins