Fluorescence properties of the three tyrosine residues in the ribose-binding protein.

doi:10.1006/bbrc.1993.2177

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Article

Fluorescence properties of the three tyrosine residues in the ribose-binding protein.

Biochemical and biophysical research communications - 30 Sept 1993

Kim D, Park C

Abstract excerpt

Three tyrosine residues but no tryptophan exist in the ribose-binding protein (RBP) of Escherichia coli. In order to assess the contribution of each tyrosine to the fluorescence properties, mutants were constructed by site-directed mutagenesis to replace tyrosines at 32, 115, and 261 by phenylala...

Topics

Carrier Proteins
Chemotaxis
Escherichia coli
Escherichia coli Proteins
Guanidine
Guanidines
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Periplasmic Binding Proteins
Protein Denaturation
Spectrometry, Fluorescence
Tyrosine

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