Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics. [electronic resource]
Producer: 20060510Description: 7479-88 p. digitalISSN:- 0021-9258
- Adenosine Diphosphate -- chemistry
- Adenosine Triphosphatases -- chemistry
- Adenosine Triphosphate -- chemistry
- Allosteric Regulation
- Allosteric Site
- Amino Acid Sequence
- Anisotropy
- Bacterial Proteins -- chemistry
- Binding Sites
- Calorimetry, Differential Scanning
- Escherichia coli -- metabolism
- Hot Temperature
- Ions
- Kinetics
- Luciferases -- metabolism
- Mass Spectrometry
- Microscopy, Fluorescence
- Molecular Chaperones -- chemistry
- Molecular Conformation
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Peptides -- chemistry
- Protein Binding
- Protein Conformation
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Sequence Homology, Amino Acid
- Spectrometry, Mass, Electrospray Ionization
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Substrate Specificity
- Temperature
- Thermodynamics
- Time Factors
- Trypsin -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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