Article
Defining the binding site of homotetrameric R67 dihydrofolate reductase and correlating binding enthalpy with catalysis.
Biochemistry - 15 Jun 2004
Strader Michael Brad, Chopra Shaileja, Jackson Michael, Smiley R Derike, Stinnett Lori, Wu Jun, Howell Elizabeth E
Abstract excerpt
R67 dihydrofolate reductase (DHFR) is a novel protein that possesses 222 symmetry. A single active site pore traverses the length of the homotetramer. Although the 222 symmetry implies that four symmetry-related binding sites should exist for each substrate as well as each cofactor, isothermal titration calorimetry (ITC) studies indicate only two molecules bind. Three possible combinations include two...
Topics
- Amino Acids
- Binding Sites
- Catalysis
- Dimerization
- Hydrogen-Ion Concentration
- Kinetics
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- NADP
- Protein Structure, Quaternary
- Tetrahydrofolate Dehydrogenase
- Thermodynamics