19F nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine

James Feeney; John E. McCormick; Christopher J. Bauer; Berry Birdsall; Claire M. Moody; Bernard A. Starkmann; Douglas W. Young; Peter Francis; Robert H. Havlin; William D. Arnold; Eric Oldfield

doi:10.1021/ja960465i

¹⁹F nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine

James Feeney, John E. McCormick, Christopher J. Bauer, Berry Birdsall, Claire M. Moody, Bernard A. Starkmann, Douglas W. Young, Peter Francis, Robert H. Havlin, William D. Arnold, Eric Oldfield

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

We have prepared Lactobacillus casei dihydrofolate reductase containing biosynthetically incorporated (2S,4S)-5-fluoroleucine ([5-F]-Leu DHFR) and have obtained its ¹H and ¹⁹F NMR spectra at 9.4 Tesla. The ¹⁹F spectrum of [5-F]-Leu DHFR showed 12 fairly sharp peaks (one containing two overlapped signals) for the 13 leucine residues in DHFR, covering a chemical shift range of 15 ppm. The large range of chemical shifts observed could not be explained solely in terms of the electrostatic field effects due to local charge fields and is thought to have a second contribution from side-chain conformational differences (γ-gauche effects) between different leucine residues, making ¹⁹F NMR of aliphatic amino acids in proteins a potentially useful new probe of protein structure.

Original language	English (US)
Pages (from-to)	8700-8706
Number of pages	7
Journal	Journal of the American Chemical Society
Volume	118
Issue number	36
DOIs	https://doi.org/10.1021/ja960465i
State	Published - Sep 11 1996

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

Online availability

10.1021/ja960465i

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Cite this

Feeney, J., McCormick, J. E., Bauer, C. J., Birdsall, B., Moody, C. M., Starkmann, B. A., Young, D. W., Francis, P., Havlin, R. H., Arnold, W. D., & Oldfield, E. (1996). ¹⁹F nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine. Journal of the American Chemical Society, 118(36), 8700-8706. https://doi.org/10.1021/ja960465i

¹⁹F nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine. / Feeney, James; McCormick, John E.; Bauer, Christopher J. et al.
In: Journal of the American Chemical Society, Vol. 118, No. 36, 11.09.1996, p. 8700-8706.

Research output: Contribution to journal › Article › peer-review

Feeney, J, McCormick, JE, Bauer, CJ, Birdsall, B, Moody, CM, Starkmann, BA, Young, DW, Francis, P, Havlin, RH, Arnold, WD & Oldfield, E 1996, '¹⁹F nuclear magnetic resonance chemical shifts of fluorine containing aliphatic amino acids in proteins: Studies on Lactobacillus casei dihydrofolate reductase containing (2S,4S)-5-fluoroleucine', Journal of the American Chemical Society, vol. 118, no. 36, pp. 8700-8706. https://doi.org/10.1021/ja960465i

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abstract = "We have prepared Lactobacillus casei dihydrofolate reductase containing biosynthetically incorporated (2S,4S)-5-fluoroleucine ([5-F]-Leu DHFR) and have obtained its 1H and 19F NMR spectra at 9.4 Tesla. The 19F spectrum of [5-F]-Leu DHFR showed 12 fairly sharp peaks (one containing two overlapped signals) for the 13 leucine residues in DHFR, covering a chemical shift range of 15 ppm. The large range of chemical shifts observed could not be explained solely in terms of the electrostatic field effects due to local charge fields and is thought to have a second contribution from side-chain conformational differences (γ-gauche effects) between different leucine residues, making 19F NMR of aliphatic amino acids in proteins a potentially useful new probe of protein structure.",

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AU - Birdsall, Berry

AU - Moody, Claire M.

AU - Starkmann, Bernard A.

AU - Young, Douglas W.

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