Markowski, Volker and Posner, Tamar B. and Loftus, Philip and Roberts, John D. (1977) Nitrogen-15 nuclear magnetic resonance of aliphatic tripeptides. Proceedings of the National Academy of Sciences of the United States of America, 74 (4). pp. 1308-1309. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:MARpnas77
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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. Nonterminal 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.
|Additional Information:||© 1977 by the National Academy of Sciences. Contributed by John D. Roberts, January 7, 1977. This is contribution no. 5490 from the Gates and Crellin Laboratories of Chemistry. These studies were supported by the U.S. Public Health Service Grant GM-11072, from the Division of General Medical Sciences, and by the National Science Foundation.|
|Subject Keywords:||peptide sequencing; 15N chemical shift; NH2-terminal amino acid; COOH-terminal amino acid; amino acid nitrogens|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||27 Nov 2007|
|Last Modified:||14 Nov 2014 19:20|
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