Journal article
Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides
Biochemical and biophysical research communications, v 42(6), pp 1148-1155
1971
PMID: 5550801
Abstract
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.
Metrics
Details
- Title
- Carbon-13 Fourier transform nuclear magnetic resonance studies of peptides
- Creators
- Murray H. Freedman - University of TorontoJack S. Cohen - NOAA Physical Sciences LaboratoryIrwin M. Chaiken - National Institute of Arthritis and Musculoskeletal and Skin Diseases
- Publication Details
- Biochemical and biophysical research communications, v 42(6), pp 1148-1155
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology; Drexel University
- Web of Science ID
- WOS:A1971I803700025
- Scopus ID
- 2-s2.0-0015232032
- Other Identifier
- 991019520534304721