Article
Design of a membrane transport protein for fluorescence spectroscopy.
Proceedings of the National Academy of Sciences of the United States of America - 1 Mar 1990
Menezes M E, Roepe P D, Kaback H R
Abstract excerpt
To modify the lac permease of Escherichia coli for fluorescence spectroscopy, six tryptophan residues at positions 10, 33, 78, 151, 171, and 223 were first replaced individually with phenylalanine by using oligonucleotide-directed site-specific mutagenesis. None of the tryptophan residues is critical for activity, as evidenced by the finding that the mutant permease molecules catalyze lactose/H+ symport almost as...
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