Search

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: 4.7 %, Completeness: 1.7 %, Completeness (bb): 0.5 % Detail

Polymer type: polypeptide(L)

Total1H
All 1.7 % (11 of 642) 1.7 % (11 of 642)
Backbone 0.5 % (1 of 216) 0.5 % (1 of 216)
Sidechain 2.3 % (10 of 426) 2.3 % (10 of 426)
Aromatic 1.8 % (1 of 56) 1.8 % (1 of 56)
Methyl 4.4 % (2 of 45) 4.4 % (2 of 45)

1. cytochrome c

TEFKAGSAKK GATLFKTHXL XHTVEKGGPH KVGPNLHGIF GRHSGQAEGY SYTDANIKKN VLWDENNMSE YLTNPXKYIP GTKMAFGGLK KEKDRNDLIT YLKKACE

Sample

Temperature 298 K, pH 4.6



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 10.1111/j.1432-1033.1991.tb15953.x ,
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