The carbonyl 13C chemical shift tensors of five peptides determined from 15N dipole-coupled chemical shift powder patterns

Terrence G. Oas, Cynthia J. Hartzell, Thomas J. McMahon, Gary P. Drobny, Frederick W. Dahlquist

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Abstract

The 13C chemical shift tensors have been determined for the glycine carbonyl carbon in a homologous series of peptides of the general form N-acetyl[1-13C]glycyl-X-amide, where X was [15N]glycine, DL-[15N]-tyrosine, L-[15N]phenylalanine and DL-[15N]alanine. The principal values and molecular orientations of the tensors were extracted from 15N dipole-coupled 13C powder spectra. The shift tensor of a powdered sample of [1-13C]glycyl[15N]glycine·HCl·H2O was determined by the same method and was found to agree to within 1 ppm in principal values and 2° in orientation with the previous single crystal measurements of R. E. Stark et al. (J. Magn. Reson. 1983, 55, 266). The shift tensors of the five peptides were found to be significantly different in both principal values and molecular orientation. However, the isotropic chemical shifts of the end-protected peptides in D2O were nearly identical. From these data it is concluded that lattice environment has a significant effect on the chemical shift tensors of peptide carbonyl carbons. An approach to approximating carbonyl 13C chemical shift tensors of peptides in proteins with use of the isotropic chemical shift in the molecule of interest is proposed. In addition, the utility of the powder pattern technique for accurately determining the chemical shift tensors of peptide carbonyl carbons is demonstrated.

Original languageEnglish (US)
Pages (from-to)5956-5962
Number of pages7
JournalJournal of the American Chemical Society
Volume109
Issue number20
StatePublished - 1987
Externally publishedYes

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Chemical shift
Powders
Peptides
Tensors
Social Values
Carbon
Molecular orientation
Glycine
Amino acids
Phenylalanine
Amides
Alanine
Tyrosine
Crystal orientation
Single crystals
Proteins
Molecules

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

The carbonyl 13C chemical shift tensors of five peptides determined from 15N dipole-coupled chemical shift powder patterns. / Oas, Terrence G.; Hartzell, Cynthia J.; McMahon, Thomas J.; Drobny, Gary P.; Dahlquist, Frederick W.

In: Journal of the American Chemical Society, Vol. 109, No. 20, 1987, p. 5956-5962.

Research output: Contribution to journalArticle

Oas, Terrence G. ; Hartzell, Cynthia J. ; McMahon, Thomas J. ; Drobny, Gary P. ; Dahlquist, Frederick W. / The carbonyl 13C chemical shift tensors of five peptides determined from 15N dipole-coupled chemical shift powder patterns. In: Journal of the American Chemical Society. 1987 ; Vol. 109, No. 20. pp. 5956-5962.
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T1 - The carbonyl 13C chemical shift tensors of five peptides determined from 15N dipole-coupled chemical shift powder patterns

AU - Oas, Terrence G.

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AU - Dahlquist, Frederick W.

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