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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1984-10-24
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pubmed:abstractText |
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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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
143
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
363-7
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6468399-Amino Acids,
pubmed-meshheading:6468399-Binding Sites,
pubmed-meshheading:6468399-Chemical Phenomena,
pubmed-meshheading:6468399-Chemistry,
pubmed-meshheading:6468399-Crystallization,
pubmed-meshheading:6468399-Energy Transfer,
pubmed-meshheading:6468399-Magnetic Resonance Spectroscopy,
pubmed-meshheading:6468399-Peptides
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pubmed:year |
1984
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pubmed:articleTitle |
van der Waals' induced 13C NMR shifts in crystalline amino acids and peptides.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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