Article
Stability and folding of precursor and mature tryptophan-substituted ribose binding protein of Escherichia coli.
Archives of biochemistry and biophysics - 1 Apr 1996
Lee H, Chi S W, Kang M, Baek K, Kim H
Abstract excerpt
A mutant ribose binding protein (RBP) of Escherichia coli was obtained by site-directed mutagenesis, replacing Phe-187 in the wild-type RBP (WT-RBP) with a Trp residue, in order to compare its stability and folding behavior with those of the WT-RBP. The equilibrium unfolding properties and the fo...
Topics
- Bacterial Proteins
- Base Sequence
- Carrier Proteins
- Chemotaxis
- Circular Dichroism
- Escherichia coli
- Escherichia coli Proteins
- Kinetics
- Models, Chemical
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Periplasmic Binding Proteins
- Protein Denaturation
- Protein Folding
- Protein Precursors
- Protein Structure, Secondary