Article
Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 1. Cooperative and noncooperative oxygen binding in Zn-substituted hemoglobin.
Biochemistry - 13 Sept 2005
Holt Jo M, Klinger Alexandra L, Yarian Connie S, Keelara Varsha, Ackers Gary K
Abstract excerpt
The complete binding cascade of human hemoglobin consists of eight partially ligated intermediates and 16 binding constants. Each intermediate binding constant can be evaluated via dimer-tetramer assembly when ligand configurations within the tetramer are fixed through the use of hemesite analogs...
Topics
- Allosteric Regulation
- Allosteric Site
- Dimerization
- Hemoglobins
- Humans
- Ions
- Mutation
- Oxygen
- Protein Binding
- Protein Structure, Quaternary
- Protein Subunits
- Zinc