Abstract

This core will create site-directed mutations of the alpha and beta globin subunits of human hemoglobin and will over-express these modified globins in E. coli using protocols that were optimized during last funding period of this Program Project Grant. In addition, strategies will be devised for producing globin subunits in which only a single type of amino acid is labeled with 13C. The frozen E. coli cell pasted produced in this core will be shipped to the Hemoglobin Assembly Core where the mutant hemoglobin tetramers will be assembled and purified.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM058890-03
Application #
6410446
Study Section
Project Start
2001-01-01
Project End
2001-12-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
3
Fiscal Year
2001
Total Cost
$176,978
Indirect Cost

  Institution

Name
University of Iowa
Department
Type
DUNS #
041294109
City
Iowa City
State
IA
Country
United States
Zip Code
52242

  Publications

Kwiatkowski, Laura D; Hui, Hilda L; Karasik, Ellen et al. (2007) Mutations of the betaN102 residue of HbA not only inhibit the ligand-linked T to Re state transition, but also profoundly affect the properties of the T state itself. Biochemistry 46:2037-49
Das, Tapan K; Dewilde, Sylvia; Friedman, Joel M et al. (2006) Multiple active site conformers in the carbon monoxide complexes of trematode hemoglobins. J Biol Chem 281:11471-9
Samuni, Uri; Roche, Camille J; Dantsker, David et al. (2006) Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation. Biochemistry 45:2820-35
Dantsker, David; Roche, Camille; Samuni, Uri et al. (2005) The position 68(E11) side chain in myoglobin regulates ligand capture, bond formation with heme iron, and internal movement into the xenon cavities. J Biol Chem 280:38740-55
Kavanaugh, Jeffrey S; Rogers, Paul H; Arnone, Arthur et al. (2005) Intersubunit interactions associated with Tyr42 alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin. Biochemistry 44:3806-20
Kavanaugh, Jeffrey S; Rogers, Paul H; Arnone, Arthur (2005) Crystallographic evidence for a new ensemble of ligand-induced allosteric transitions in hemoglobin: the T-to-T(high) quaternary transitions. Biochemistry 44:6101-21
Dantsker, David; Samuni, Uri; Ouellet, Yannick et al. (2004) Viscosity-dependent relaxation significantly modulates the kinetics of CO recombination in the truncated hemoglobin TrHbN from Mycobacterium tuberculosis. J Biol Chem 279:38844-53
Tsuneshige, Antonio; Kanaori, Kenji; Samuni, Uri et al. (2004) Semihemoglobins, high oxygen affinity dimeric forms of human hemoglobin respond efficiently to allosteric effectors without forming tetramers. J Biol Chem 279:48959-67
Wheeler, Korin E; Lees, Nicholas S; Gurbiel, Ryszard J et al. (2004) Electrostatic influence on rotational mobilities of sol-gel-encapsulated solutes by NMR and EPR spectroscopies. J Am Chem Soc 126:13459-63
Chan, Nei-Li; Kavanaugh, Jeffrey S; Rogers, Paul H et al. (2004) Crystallographic analysis of the interaction of nitric oxide with quaternary-T human hemoglobin. Biochemistry 43:118-32

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