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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
Authors
Moench, S.J., Shi, T., Satterlee, J.D.
Assembly
cytochrome c
Entity
1. cytochrome c (polymer), 107 monomers, 12941.24 Da Detail

TEFKAGSAKK GATLFKTHXL XHTVEKGGPH KVGPNLHGIF GRHSGQAEGY SYTDANIKKN VLWDENNMSE YLTNPXKYIP GTKMAFGGLK KEKDRNDLIT YLKKACE


Formula weight
12941.24 Da
Source organism
Saccharomyces cerevisiae
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 12.1 %, Completeness: 5.5 %, Completeness (bb): 5.1 % Detail

Polymer type: polypeptide(L)

Total1H
All 5.5 % (35 of 642) 5.5 % (35 of 642)
Backbone 5.1 % (11 of 216) 5.1 % (11 of 216)
Sidechain 5.6 % (24 of 426) 5.6 % (24 of 426)
Aromatic 1.8 % (1 of 56) 1.8 % (1 of 56)
Methyl 6.7 % (3 of 45) 6.7 % (3 of 45)

1. cytochrome c

TEFKAGSAKK GATLFKTHXL XHTVEKGGPH KVGPNLHGIF GRHSGQAEGY SYTDANIKKN VLWDENNMSE YLTNPXKYIP GTKMAFGGLK KEKDRNDLIT YLKKACE

Sample

Temperature 298 K, pH 6.4



Release date
1995-07-30
Citation
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
Moench, S.J., Shi, T., Satterlee, J.D.
Eur. J. Biochem. (1991), 197, 631-641, PubMed 1851480 , DOI: ,
Related entities 1. cytochrome c, : 231 entities Detail
Interaction partners 1. cytochrome c, : 4 interactors Detail
Experiments performed 1 experiments Detail
Chemical shift validation 3 contents Detail