Open AccessNuclear magnetic resonance studies of slowly exchanging peptide protons in cytochrome c in aqueous solution.
Author(s) -
Dinshaw J. Patel,
Lita L. Canuel
Publication year - 1976
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.73.5.1398
Subject(s) - aqueous solution , nuclear magnetic resonance , chemistry , proton , cytochrome c , resonance (particle physics) , sulfonate , spectral line , cytochrome , sodium , biochemistry , physics , atomic physics , organic chemistry , mitochondrion , nuclear physics , astronomy , enzyme
The slowly exchanging protons in oxidized and reduced horse heart cytochrome c (D20, uncorrected pH meter reading 6.5 room temperature) have been monitored by recording the 270 and 360 MHz proton nuclear magnetic resonance spectra of the reduced protein between 5 and 11 parts per million downfield from 2,2-dimethyl-2-silapentane-5-sulfonate.