Article
Effects of metal binding affinity on the chemical and thermal stability of site-directed mutants of rat oncomodulin.
Biophysical chemistry - 20 Apr 1998
Zheng L, Hogue C W, Brennan J D
Abstract excerpt
Tryptophan fluorescence was used to study the stability and unfolding behavior of several single tryptophan mutants of the metal-binding protein rat oncomodulin (OM); F102W, Y57W, Y65W and the engineered protein CDOM33 which had the 12 residues of the CD loop replaced with a more potent metal bin...
Topics
- Acrylamide
- Acrylamides
- Animals
- Calcium
- Calcium-Binding Proteins
- Fluorescence
- Guanidine
- Hydrogen Bonding
- Metals
- Mutagenesis, Site-Directed
- Mutation
- Neoplasm Proteins
- Protein Binding
- Protein Denaturation
- Protein Folding
- Protein Structure, Secondary
- Rats
- Temperature