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
- 1 January 1996
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 118 (36) , 8700-8706
- https://doi.org/10.1021/ja960465i
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Stereospecific assignments of the leucine methyl resonances in the 1H NMR spectrum of Lactobacillus casei dihydrofolate reductaseFEBS Letters, 1993
- Efficient implementation of the gauge-independent atomic orbital method for NMR chemical shift calculationsJournal of the American Chemical Society, 1990
- Preparation and Properties of Nalpha-Di-tert-Butoxycarbonyl Amino Acids. Applicability in the Synthesis of Leu-Enkephalin.Acta Chemica Scandinavica, 1990
- Dihydrofolate reductaseJournal of Molecular Biology, 1986
- NMR studies of fluorophenylalanine‐containing carbonic anhydraseFEBS Letters, 1986
- Activation of methane by iridium complexesJournal of the American Chemical Society, 1983
- Proximity of two tryptophan residues in dihydrofolate reductase determined by 19F NMRNature, 1978
- Nuclear magnetic resonance and fluorescence studies of substrate-induced conformational changes of histidine-binding protein J of Salmonella typhimuriumBiochemistry, 1977
- 4-Fluorotryptophan alkaline phosphatase from E.coli: Preparation, properties, and 19F NMR spectrumBiochemical and Biophysical Research Communications, 1976
- Ion Pairs in EliminationJournal of the American Chemical Society, 1963