Article
Site mutations disrupt inter-helical H-bonds (alpha14W-alpha67T and beta15W-beta72S) involved in kinetic steps in the hemoglobin R-->T transition without altering the free energies of oxygenation.
Biophysical chemistry - 1 Jan 2003
Tsai Ching-Hsuan, Simplaceanu Virgil, Ho Nancy T, Shen Tong-Jian, Wang Daojing, Spiro Thomas G, Ho Chien
Abstract excerpt
Three recombinant mutant hemoglobins (rHbs) of human normal adult hemoglobin (Hb A), rHb (alphaT67V), rHb (betaS72A), and rHb (alphaT67V, betaS72A), have been constructed to test the role of the tertiary intra-subunit H-bonds between alpha67T and alpha14W and between beta72S and beta15W in the cooperative oxygenation of Hb A. Oxygen-binding studies in 0.1 M sodium phosphate buffer at 29 degrees C show that rHb...
Topics
- Adult
- Energy Metabolism
- Escherichia coli
- Hemoglobin A
- Humans
- Hydrogen Bonding
- Hydrogen-Ion Concentration
- Kinetics
- Magnetic Resonance Spectroscopy
- Mutation