Published January 1, 1980
| public
Journal Article
Nitrogen-15 magnetic resonance spectroscopy. Natural-abundance spectra of isomeric homooligopeptides of L-norvaline and L-valine to the tetramers
Abstract
The ^(15)N NMR shifts of chemically and optically pure N- and C-protected homooligopeptides derived from L-norvaline and L-valine to the tetramers have been determined at the natural-abundance level of ^(15)N by using the Fourier-transform technique. The shift effects produced by increasing the chain length and temperature, as well as changing the solvent from a hydrogen-bonding donor to a hydrogen-bonding acceptor and replacing the linear side chain (as in the norvaline peptides) by a β branched side chain (as in the valine peptides), are discussed.
Additional Information
© 1980 American Chemical Society. Received June 11, 1979. The portion of the research reported in this paper that was carried out at the California Institute of Technology was supported by the National Science Foundation and by the Public Health Service, Research Grant No. GM-11072 from the Division of General Medical Sciences. The syntheses and characterizations reported here were carried out at the University of Padua and supported by the CNR, Italy.Additional details
- Eprint ID
- 60832
- Resolver ID
- CaltechAUTHORS:20151007-073140400
- NSF
- GM-11072
- U.S. Public Health Service (USPHS)
- Created
-
2015-10-07Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Gates and Crellin Laboratories of Chemistry
- Other Numbering System Identifier
- 6113