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Current hemoglobin research

Frank Ferrone Lab
-study of the kinetics and thermodynamics of polymer formation of the HbS

Joel M. Friedman  M.D., Ph.D. Lab -- Albert Einstein College of Medicine
study of the structure and dynamic elements in hemoglobin and myoglobin that control oxygen binding properties in these two model protein systems. Dr. Friedman is director of a project with a multidisciplinary effort to create acellular hemoglobin based blood substitutes for clinical use

Rhoda Elison Hirsch, Ph.D. Lab -- Albert Einstein College of Medicine
-study of interactions of 6 hemoglobin mutants with natural or synthetic allosteric effectors and red blood cell components providing key information about hemoglobin communication and regions imparting unique stability to hemoglobin molecules important for the development of HBOCs.

Dr. Robin  B Briehl Lab -- Albert Einstein College of Medicine
-study of HbS polymerization and gelation by physical chemicals methods like  light scattering, ultracentrifugation, viscometry, NMR. The lab studies projects such as mechanisms of fiber depolymerization; microrheology of fibers including moduli and persistence lengths; the effects of site specific mutations on equilibria, kinetics, structure and mechanisms; delineation of the molecular sites responsible for cross-linking and nucleation; the role of the red cell membrane

Gary K. Ackers Lab --Washington University School of Medicine
-study of the molecular regulation of human hemoglobin, how protein assemblies self-regulate in response to environmental signals.

Jonathan Stamler Lab
- investigates the interaction of nitric oxide with proteins. One of which is cysteine 93 in human hemoglobin. Affinity of cysteine 93 for NO is high in the R (or oxy) structure and low in the alternative T (or deoxy) structure. Studies point to NO's unsuspected role in the respiratory cycle by ensuring adequate blood flow to tissues.

Spiro Lab --Princeton University
-study the involvement of inorganic elements such as iron, cobalt, copper, and zinc in biological processes. Particularly the study of NO and CO signaling molecules whose activity is modulated by Fe++ of the heme proteins

Irina M. Russu Lab -- Wesleyan University
-study of the molecular mechanisms responsible for the cooperative binding of oxygen to human hemoglobin and for the allosteric effects of other components of the red blood cells upon hemoglobin function