Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Modified Research Career Development Award (K04)
Project #
7K04HL001758-04
Application #
3074015
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1989-09-30
Project End
1991-09-29
Budget Start
1989-09-30
Budget End
1990-09-29
Support Year
4
Fiscal Year
1989
Total Cost
Indirect Cost
Name
Washington State University
Department
Type
Schools of Arts and Sciences
DUNS #
041485301
City
Pullman
State
WA
Country
United States
Zip Code
99164
Aiken, N R; Galey, W R; Satterlee, J D (1995) A peroxidative model of human erythrocyte intracellular Ca2+ changes with in vivo cell aging: measurement by 19F-NMR spectroscopy. Biochim Biophys Acta 1270:52-7
Moench, S J; Chroni, S; Lou, B S et al. (1992) Proton NMR comparison of noncovalent and covalently cross-linked complexes of cytochrome c peroxidase with horse, tuna, and yeast ferricytochromes c. Biochemistry 31:3661-70
Russell, D J; Pearce, G; Ryan, C A et al. (1992) Proton NMR assignments of systemin. J Protein Chem 11:265-74
Aiken, N R; Satterlee, J D; Galey, W R (1992) Measurement of intracellular Ca2+ in young and old human erythrocytes using 19F-NMR spectroscopy. Biochim Biophys Acta 1136:155-60
Satterlee, J D; Russell, D J; Erman, J E (1991) Proton homonuclear correlated spectroscopy as an assignment tool for hyperfine-shifted resonances in medium-sized paramagnetic proteins: cyanide-ligated yeast cytochrome c peroxidase as an example. Biochemistry 30:9072-7
Satterlee, J D; Erman, J E (1991) Proton NMR assignments of heme contacts and catalytically implicated amino acids in cyanide-ligated cytochrome c peroxidase determined from one- and two-dimensional nuclear Overhauser effects. Biochemistry 30:4398-405
Busse, S C; Moench, S J; Satterlee, J D (1990) One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c. Biophys J 58:45-51
Satterlee, J D; Erman, J E; Mauro, J M et al. (1990) Comparative proton NMR analysis of wild-type cytochrome c peroxidase from yeast, the recombinant enzyme from Escherichia coli, and an Asp-235----Asn-235 mutant. Biochemistry 29:8797-804
Simons, P C; Satterlee, J D (1989) cDNA cloning and predicted amino acid sequence of Glycera dibranchiata monomer hemoglobin IV. Biochemistry 28:8525-30
Constantinidis, I; Kandler, R L; Satterlee, J D (1989) Purity of Glycera dibranchiata monomer hemoglobin components III and IV determined by isoelectric focusing. Comp Biochem Physiol B 92:619-22

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