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Nitrogen-15 nuclear magnetic resonance of aliphatic tripeptides.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Markowski, V. Posner, T. B. Loftus, Peter J. Roberts, John D. |
| Copyright Year | 1977 |
| Abstract | The 15N chemical shifts of eight aliphatic tripeptides have been measured at the natural-abundance level. For a given tripeptide, the resonances of the COOH-terminal and NH2-terminal amino acids can be identified by measurements at low or high pH. The shifts of the NH2-terminal amino acid nitrogens are essentially independent of the amino acids in the rest of the peptide. The shifts of the other nitrogens are characteristic of the amino acids themselves and of the immediately preceding amino acid toward the NH2 terminus. Non-terminal amide nitrogens have shifts of about 6 ppm upfield of COOH-terminal amide nitrogens at the isoelectric point of measurement. 15N chemical shifts appear to have considerable potential value for peptide sequencing. |
| Starting Page | 313 |
| Ending Page | 316 |
| Page Count | 4 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://authors.library.caltech.edu/9209/1/MARpnas77.pdf |
| PubMed reference number | 16259v1 |
| Volume Number | 74 |
| Issue Number | 4 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Amino Acid Metabolism, Inborn Errors Amino Acids Amino Acids, Branched-Chain Biopolymer Sequencing Isoelectric Point Mechlorethamine aliphatic aldoxime dehydratase activity indoleacetic acid amide conjugate biosynthetic process part per million (ppm) |
| Content Type | Text |
| Resource Type | Article |
