Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides

Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides

The carbon-13 nuclear magnetic resonance (CMR) spectra of several small peptides have been obtained at 25.1 MHz and natural abundance of 13C using the Fourier transform technique with proton noise decoupling. Chemical shift values have been studied as a function of pH. The peptide corresponding to t...

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Veröffentlicht in:Biochemical and biophysical research communications 1971-03, Vol.42 (6), p.1148-1155
Hauptverfasser: Freedman, Murray H., Cohen, Jack S., Chaiken, Irwin M.
Format: Artikel
Sprache:eng
Schlagworte:
Carbon Isotopes
Computers
Histidine - analysis
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Peptides - analysis
Phenylalanine - analysis
Ribonucleases - analysis
Stereoisomerism
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Zusammenfassung:The carbon-13 nuclear magnetic resonance (CMR) spectra of several small peptides have been obtained at 25.1 MHz and natural abundance of 13C using the Fourier transform technique with proton noise decoupling. Chemical shift values have been studied as a function of pH. The peptide corresponding to the 1–15 sequence of ribonuclease has been synthesized both with normal and 15% 13C enriched Phe in position 8, and the CMR spectra of these two products are compared.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(71)90025-8