Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics.

Fernández-Sáiz, Vanesa

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