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 crit...
Topics
- Amino Acid Sequence
- Base Sequence
- Biological Transport, Active
- Cell Membrane
- Codon
- Escherichia coli
- Escherichia coli Proteins
- Kinetics
- Membrane Proteins
- Membrane Transport Proteins
- Molecular Sequence Data
- Monosaccharide Transport Proteins
- Mutation
- Protein Conformation
- Spectrometry, Fluorescence
- Symporters