Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics. [electronic resource]
- The Journal of biological chemistry Mar 2006
- 7479-88 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.M512744200 doi
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