Article
Structure, dynamics, and catalytic function of dihydrofolate reductase.
Annual review of biophysics and biomolecular structure - 1 Jan 2004
Schnell Jason R, Dyson H Jane, Wright Peter E
Abstract excerpt
Molecular motions are widely regarded as contributing factors in many aspects of protein function. The enzyme dihydrofolate reductase (DHFR), and particularly that from Escherichia coli, has become an important system for investigating the linkage between protein dynamics and catalytic function, both because of the location and timescales of the motions observed and because of the availability of a large amount...
Topics
- Amino Acid Substitution
- Catalysis
- Enzyme Activation
- Escherichia coli
- Kinetics
- Models, Molecular
- Motion
- Mutation
- Protein Conformation
- Protein Folding
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Structure-Activity Relationship
- Tetrahydrofolate Dehydrogenase