van der Waals' induced 13C NMR shifts in crystalline amino acids and peptides.

Research output: Contribution to journalArticle

Abstract

Recent reports in the literature of solid-state 13C nuclear magnetic resonance (NMR) spectra of crystalline L-alanine [Naito, A., Ganapathy, S., Akasaka, K., and McDonnell, C. A. (1981) J. Chem. Phys. 74, 3190-3197] and L-leucine [Frey, M. H. and Opella, S. J. (1980) J. Chem. Soc. Chem. Commun., 474-475], recorded with cross-polarization and magic-angle spinning (CP-MAS), show downfield resonance shifts of several parts per million in their side-chain methyl groups, relative to their resonance positions in aqueous solution. Similar findings are reported here for crystalline aliphatic amino acids and L-alanine peptides, including tetra(L-alanine), which show similar, specific downfield shifts in their side-chain methyl resonances. Coupled with X-ray crystallographic data of these compounds, and previous gas and solution-phase 13C NMR studies, the CP-MAS 13C NMR data indicate that these downfield shifts are a result of van der Waals' interactions. This group have reported similar van der Waals' induced shifts of the same magnitude for 13C resonances of the side-chain methyl groups of 13C-enriched tetra(L-alanine) upon binding to high-affinity Fab' fragments of heterogeneous sheep anti-[poly(L-alanine)] antibodies in aqueous solution [Geller, S., Wei, S. C., Shkuda, G. K., Marcus, D. M., and Brewer, C. F. (1980) Biochemistry 19, 3614-3623]. The above findings show that van der Waals' induced 13C NMR shifts of similar magnitudes can be detected in specific antibody-hapten complexes and the side chains of crystalline aliphatic amino acids and peptides. The results also indicate that water possesses relatively little attractive van der Waals' interactions with aliphatic molecules.

Original languageEnglish (US)
Pages (from-to)363-367
Number of pages5
JournalEuropean Journal of Biochemistry
Volume143
Issue number2
StatePublished - Sep 3 1984

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Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Crystalline materials
Amino Acids
Peptides
Magic angle spinning
Alanine
Fatty Acids
Polarization
Immunoglobulin Fab Fragments
Biochemistry
Antibodies
Haptens
Leucine
Sheep
Gases
X-Rays
X rays
Molecules
Water

ASJC Scopus subject areas

  • Biochemistry

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van der Waals' induced 13C NMR shifts in crystalline amino acids and peptides. / Brewer, Curtis F.

In: European Journal of Biochemistry, Vol. 143, No. 2, 03.09.1984, p. 363-367.

Research output: Contribution to journalArticle

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abstract = "Recent reports in the literature of solid-state 13C nuclear magnetic resonance (NMR) spectra of crystalline L-alanine [Naito, A., Ganapathy, S., Akasaka, K., and McDonnell, C. A. (1981) J. Chem. Phys. 74, 3190-3197] and L-leucine [Frey, M. H. and Opella, S. J. (1980) J. Chem. Soc. Chem. Commun., 474-475], recorded with cross-polarization and magic-angle spinning (CP-MAS), show downfield resonance shifts of several parts per million in their side-chain methyl groups, relative to their resonance positions in aqueous solution. Similar findings are reported here for crystalline aliphatic amino acids and L-alanine peptides, including tetra(L-alanine), which show similar, specific downfield shifts in their side-chain methyl resonances. Coupled with X-ray crystallographic data of these compounds, and previous gas and solution-phase 13C NMR studies, the CP-MAS 13C NMR data indicate that these downfield shifts are a result of van der Waals' interactions. This group have reported similar van der Waals' induced shifts of the same magnitude for 13C resonances of the side-chain methyl groups of 13C-enriched tetra(L-alanine) upon binding to high-affinity Fab' fragments of heterogeneous sheep anti-[poly(L-alanine)] antibodies in aqueous solution [Geller, S., Wei, S. C., Shkuda, G. K., Marcus, D. M., and Brewer, C. F. (1980) Biochemistry 19, 3614-3623]. The above findings show that van der Waals' induced 13C NMR shifts of similar magnitudes can be detected in specific antibody-hapten complexes and the side chains of crystalline aliphatic amino acids and peptides. The results also indicate that water possesses relatively little attractive van der Waals' interactions with aliphatic molecules.",
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