| Nitrogen-15 nuclear magnetic resonance of aliphatic tripeptides. | |
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MedLine Citation:
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PMID: 16259 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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V Markowski; T B Posner; P Loftus; J D Roberts |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 74 ISSN: 0027-8424 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 1977 Apr |
Date Detail:
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Created Date: 1977-06-30 Completed Date: 1977-06-30 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 1308-9 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Dipeptides Hydrogen-Ion Concentration Magnetic Resonance Spectroscopy Nitrogen Isotopes Oligopeptides* |
| Chemical | |
Reg. No./Substance:
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0/Dipeptides; 0/Nitrogen Isotopes; 0/Oligopeptides |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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