| Entry ID |
Link Type |
Entity ID |
Title |
|
216
|
Sequence mapping |
1 |
1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and
Iron-Hexacyanide-Mediated Electron Exchange |
|
220
|
Sequence mapping |
1 |
1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and
Iron-Hexacyanide-Mediated Electron Exchange |
|
224
|
Sequence mapping |
1 |
1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and
Iron-Hexacyanide-Mediated Electron Exchange |
|
243
|
Sequence mapping |
1 |
Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal
Helix |
|
244
|
Sequence mapping |
1 |
Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal
Helix |
|
274
|
Sequence mapping |
1 |
Proton Resonance Assignments of Horse Ferricytochrome c |
|
285
|
Sequence mapping |
1 |
Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of
horse ferricytochrome c |
|
286
|
Sequence mapping |
1 |
Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of
horse ferricytochrome c |
|
316
|
Sequence mapping |
1 |
Proton NMR studies of horse ferricytochrome c Completion of the assignment of
the well resolved hyperfine shifted resonances |
|
317
|
Sequence mapping |
1 |
Proton NMR studies of horse ferricytochrome c Completion of the assignment of
the well resolved hyperfine shifted resonances |
|
336
|
Sequence mapping |
1 |
1H-NMR studies of structural homologies between the heme environments in horse
cytochrome c and in cytochrome c-552 from Euglena gracilis |
|
436
|
Sequence mapping |
1 |
Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by
Two-Dimensional Proton NMR |
|
437
|
Sequence mapping |
1 |
Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by
Two-Dimensional Proton NMR |
|
438
|
Sequence mapping |
1 |
Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by
Two-Dimensional Proton NMR |
|
439
|
Sequence mapping |
1 |
Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by
Two-Dimensional Proton NMR |
|
1058
|
Sequence mapping |
1 |
Proton Magnetic Resonance Studies of Horse Cytochrome c |
|
1107
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1108
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1109
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1110
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1111
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1112
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1113
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1114
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1116
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
|
1170
|
Sequence mapping |
1 |
Assignment of Proton Resonances, Identification of Secondary Structural
Elements, and Analysis of Backbone Chemical Shifts for the C102T Variant of
Yeast Iso-1-cytochrome c and Horse Cytochrome c |
|
1171
|
Sequence mapping |
1 |
Assignment of Proton Resonances, Identification of Secondary Structural
Elements, and Analysis of Backbone Chemical Shifts for the C102T Variant of
Yeast Iso-1-cytochrome c and Horse Cytochrome c |
|
1404
|
Sequence mapping |
1 |
A systematic approach towards the complete assignment of 13C resonances for horse ferrocytochrome c |
|
1736
|
Sequence mapping |
1 |
Heteronuclear Multiple-Quantum Coherence NMR Spectroscopy of Paramagnetic Heme
and Cytochrome c-551 |
|
1783
|
Sequence mapping |
1 |
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 |
|
1785
|
Sequence mapping |
1 |
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 |
|
1787
|
Sequence mapping |
1 |
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 |
|
1789
|
Sequence mapping |
1 |
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 |
|
2366
|
Sequence mapping |
1 |
Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c |
|
2367
|
Sequence mapping |
1 |
Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c |
|
2368
|
Sequence mapping |
1 |
Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c |
|
4189
|
Sequence mapping |
1 |
Solution Structure of Reduced Horse Heart Cytochrome c |
|
4805
|
Sequence mapping |
1 |
1H, 13C and 15N chemical shifts of bovine ferric cytochrome b5 in complex with
horse heart ferric cytochrome c |
|
4808
|
Sequence mapping |
1 |
1H, 13C and 15N chemical shifts of bovine ferrous cytochrome b5 in complex with
horse heart ferrous cytochrome c |
|
4809
|
Sequence mapping |
1 |
1H, 13C and 15N chemical shifts of bovine ferrous cytochrome b5-N17D in complex
with horse heart ferrous cytochrome c |
|
4810
|
Sequence mapping |
1 |
1H, 13C and 15N chemical shifts of bovine ferric cytochrome b5 in complex with
horse heart ferric cytochrome c |
|
16759
|
Sequence mapping |
1 |
Mapping of the anion binding sites on cytochrome c by differential chemical modification of lysine residues |
|
17120
|
Sequence mapping |
1 |
Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignments by two-dimensional NMR |
|
17215
|
Sequence mapping |
2 |
13C NMR Spectroscopic and X-ray Crystallographic Study of the Role Played by Mitochondrial Cytochrome b5 Heme Propionates in the Electrostatic Binding to Cytochrome c |
|
17847
|
Sequence mapping |
1 |
Backbone 1H, 13C, and 15N chemical shift assignments of oxidized horse heart cytochrome c |
|
17848
|
Sequence mapping |
1 |
Backbone 1H, 13C, and 15N chemical shift assignments of reduced horse heart cytochrome c |
|
25640
|
PDB cross-referencing |
1 |
STRUCTURE OF OXIDIZED HORSE HEART CYTOCHROME C ENCAPSULATED IN REVERSE MICELLES |
|
27556
|
Author supplied |
1 |
NMR chemical shifts of horse heart cytochrome c bound to 1:1 (molar) TOCL/DOPC vesicles. |
