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
| Autor: | William D. Arnold, Douglas W. Young, Bernard A Starkmann, John E McCormick, Peter S. Francis, Christopher J Bauer, Claire M Moody, Robert H. Havlin, J. Feeney, Eric Oldfield, Berry Birdsall |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
chemistry.chemical_classification
Lactobacillus casei biology Stereochemistry Chemical shift Fluorine containing General Chemistry Fluorine-19 NMR biology.organism_classification Biochemistry Catalysis Amino acid Colloid and Surface Chemistry Protein structure chemistry Dihydrofolate reductase biology.protein Leucine |
| Zdroj: | Journal of the American Chemical Society. 118:8700-8706 |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|