Multistep mechanism of substrate binding determines chaperone activity of Hsp70. [electronic resource]
Producer: 20000721Description: 586-93 p. digitalISSN:- 1072-8368
- Adenosine Diphosphate -- metabolism
- Adenosine Triphosphatases -- chemistry
- Adenosine Triphosphate -- metabolism
- Allosteric Site -- drug effects
- Bacterial Proteins -- chemistry
- Catalytic Domain
- Enzyme Activation
- Escherichia coli -- chemistry
- Escherichia coli Proteins
- Genetic Complementation Test
- HSP70 Heat-Shock Proteins -- chemistry
- Heat-Shock Proteins -- metabolism
- Hydrolysis -- drug effects
- Kinetics
- Models, Biological
- Models, Molecular
- Molecular Chaperones -- chemistry
- Mutation -- genetics
- Phenotype
- Protein Binding -- drug effects
- Protein Structure, Secondary -- drug effects
- Sigma Factor
- Thermodynamics
- Transcription Factors -- metabolism
No physical items for this record
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
There are no comments on this title.
Log in to your account to post a comment.