Nuclear magnetic resonance studies of slowly exchanging peptide protons in cytochrome c in aqueous solution. | Zendy

Dinshaw J. Patel | Zendy; L L Canuel | Zendy

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Nuclear magnetic resonance studies of slowly exchanging peptide protons in cytochrome c in aqueous solution.

Author(s) -

Dinshaw J. Patel,

L L Canuel

Publication year - 1976

Publication title -

proceedings of the national academy of sciences

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.

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