Current
hemoglobin research
Frank
Ferrone Lab
-study of the kinetics and thermodynamics of polymer formation of the
HbS
http://www.physics.drexel.edu/~ferrone/Frank_Ferrone_Research.html
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
http://www.aecom.yu.edu/home/sggd/faculty/friedman.htm
Rhoda
Elison Hirsch, Ph.D. Lab -- Albert Einstein College of Medicine
-study of interactions of ß6 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.
http://www.aecom.yu.edu/home/sggd/faculty/hirsch.htm
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
http://www.aecom.yu.edu/home/sggd/faculty/briehl.htm
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.
http://biochem.wustl.edu/~ackers/
Jonathan
Stamler Lab
- investigates the interaction of nitric oxide with proteins. One of which
is cysteine ß93 in human hemoglobin. Affinity
of cysteine ß93 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.
http://www.hhmi.org/research/investigators/stamler.html
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
http://www.princeton.edu/~spirolab/
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
http://www.wesleyan.edu/chem/faculty/russu/index.html
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