• Friedman, Joel M. (PI)
  • Ackers, Gary (PI)
  • Noble, Robert (PI)
  • Arnone, Arthur (PI)
  • Sligar, Stephen G. (PI)
  • Walder, Joseph (PI)
  • Hoffman, Brian (PI)
  • Walder, Roxanne (PI)
  • Rose, George (PI)
  • Noble, Robert (PI)
  • Arnone, Arthur (PI)
  • Sligar, Stephen G. (PI)
  • Walder, Joseph (PI)
  • Hoffman, Brian (PI)
  • Walder, Roxanne (PI)
  • Rose, George (PI)

Project: Research project

Project Details


The central goal is to develop a better understanding of the factors and
elements which control functional behavior of the human hemoglobin
molecule. The approach that will be employed 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 research groups that have
complementary areas of expertise and a common focus of interest on
mechanisms of hemoglobin function and structure. In order to achieve this
concentrated effort, it has been necessary to bring together individuals
from a number of different institutions. (We know of no single institution
with a comparable level of interest and expertise in this field.) This
group has a proven track record of productive collaboration during the
previous period of this grant. Other strengths include: a) efficiently
functioning core facilities that have been developed under the current
funding of this Program Project for production of large amounts of
genetically engineered hemoglobin variants. b) 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 different laboratories will be 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 cell substitute materials.
Effective start/end date12/1/932/28/99


  • Medicine(all)


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