Article
Interfacial and distal-heme pocket mutations exhibit additive effects on the structure and function of hemoglobin.
Biochemistry - 7 Oct 2008
Maillett David H, Simplaceanu Virgil, Shen Tong-Jian, Ho Nancy T, Olson John S, Ho Chien
Abstract excerpt
Protein engineering strategies seek to develop a hemoglobin-based oxygen carrier with optimized functional properties, including (i) an appropriate O 2 affinity, (ii) high cooperativity, (iii) limited NO reactivity, and (iv) a diminished rate of auto-oxidation. The mutations alphaL29F, alphaL29W, alphaV96W and betaN108K individually impart some of these traits and in combinations produce hemoglobin molecules with...
Topics
- Heme
- Hemoglobins
- Humans
- Kinetics
- Mutation
- Oxygen
- Protein Binding
- Recombinant Proteins