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Protein Science, Vol 9, Issue 12 2573-2576, Copyright © 2000 by Cold Spring Harbor Laboratory Press
JOURNAL ARTICLE |
LA Luck and C Johnson
Department of Chemistry, Clarkson University, Potsdam, New York 13699, USA. luckla@clarkson.edu
The binding capacity of the L-leucine receptor from Escherichia coli was measured with L-phenylalanine and 4-fluoro-L-phenylalanine as substrates by fluorescence. The apparent dissociation constants (KD) for L-leucine, L-phenylalanine, and 4-fluoro-L-phenylalanine are 0.40, 0.18, and 0.26 respectively. 19F NMR data show protein-induced shifts for the 4-fluoro-L-phenylalanine peak and 3-fluoro-L-phenylalanine when receptor is present. Evidence points to the binding of only the L-isomers of these fluorine analogs.
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