Entry ID |
Original Release date |
Data summary |
Entry Title |
Citation Title |
Authors |
4038 |
1998-06-13 |
Chemical Shifts: 2 sets |
Detailed NMR Analysis of the Heme-Protein Interactions in Component IV Glycera Dibranchiata Monomeric Hemoglobin-CO |
Detailed NMR Analysis of the Heme-Protein Interactions in Component IV Glycera dibranchiata Monomeric Hemoglobin-CO
|
Brian F Volkman, James D Satterlee, John L Markley, Steven L Alam |
1839 |
1995-07-31 |
Chemical Shifts: 1 set |
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 |
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
|
James D Satterlee, James E Erman |
1841 |
1999-06-14 |
Chemical Shifts: 1 set |
Proton Hyperfine Resonance Assignments in Cyanide-ligated Cytochrome c Peroxidase Using the Nuclear Overhauser Effect |
Proton Hyperfine Resonance Assignments in Cyanide-ligated Cytochrome c Peroxidase Using the Nuclear Overhauser Effect
|
James D Satterlee, James E Erman |
1889 |
1999-06-14 |
Chemical Shifts: 1 set |
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 |
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
|
David J Russell, James D Satterlee, James E Erman |
1779 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1781 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1783 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1785 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1787 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1789 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1791 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1793 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1795 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1797 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
2488 |
1995-07-31 |
Chemical Shifts: 1 set |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
|
Daina Z Avizonis, James D Satterlee, Susan J Moench |
2489 |
1995-07-31 |
Chemical Shifts: 1 set |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect |
Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect
|
Daina Z Avizonis, James D Satterlee, Susan J Moench |
330 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer
|
James D Satterlee, Susan J Moench |
331 |
Unknown |
Chemical Shifts: 1 set |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer |
Proton NMR Comparison of the Saccharomyces cerevisiae Ferricytochrome c Isozyme-1 Monomer and Covalent Disulfide Dimer
|
James D Satterlee, Susan J Moench |
499 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c
|
James D Satterlee, Susan J Moench |
1192 |
1995-07-31 |
Chemical Shifts: 1 set |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c
|
James D Satterlee, Scott C Busse, Susan J Moench |
500 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c |
Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c
|
James D Satterlee, Susan J Moench |
1194 |
1995-07-31 |
Chemical Shifts: 1 set |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c |
One- and two-dimensional proton NMR studies of cys-102 S-methylated yeast isozyme-1 ferricytochrome c
|
James D Satterlee, Scott C Busse, Susan J Moench |
1775 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |
1777 |
1995-07-31 |
Chemical Shifts: 1 set |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c |
Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c
|
James D Satterlee, Susan J Moench, Ting-Mei Shi |