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19F Nuclear Magnetic Resonance Chemical Shifts of Flourine Containing Aliphatic Amino Acids in Proteins: Studies on Lactobacillus casei DihydrofolateReductase Containing (2S 4S )-5-Flouroleucine II

journal contribution
posted on 2023-06-08, 08:35 authored by 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
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 (?-gauche effects) between different leucine residues, making 19F NMR of aliphatic amino acids in proteins a potentially useful new probe of protein structure.

History

Publication status

  • Published

Journal

Journal of the American Chemical Society

ISSN

0002-7863

Publisher

ACS Publications

Volume

118

Page range

8700 - 8706

ISBN

0002-7863

Department affiliated with

  • Chemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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