Gary K. Ackers, Ph.D. (Director)

DEPARTMENT OF Biochemistry & Molecular Biophysics
Keywords: cell biology, genetics, hemoglobin, protein 3D structure

The central goal of this program project is to better understand the factors and elements that control functional behavior of the human hemoglobin molecule. The approach that we use is to identify the roles of amino acid side chains in the molecule's normal functioning by residue substitution at specifically targeted sites, coupled with extensive structural and functional characterization of the resulting hemoglobin molecules.

This program project brings together seven groups of scientists from leading research universities that have complementary areas of expertise and a common interest in the mechanisms of hemoglobin function and structure. Core facilities are maintained for the production of large amounts of genetically engineered hemoglobin variants, as are facilities and expertise for detailed, systematic characterization of structural (i.e., X-ray, spectroscopic and theoretical) and functional (kinetic and thermodynamic) properties of hemoglobin.

Work in the various laboratories is coordinated through planned collaborations, exchanges of materials and personnel and quarterly meetings. Results will be synthesized into a predictive model of the hemoglobin mechanism. This new level of understanding may permit the rational design of structurally modified hemoglobins with desired properties, including potential red blood cell substitute materials.