Ligand-induced conformational and structural dynamics changes in Escherichia coli cyclic AMP receptor protein

Keyphrases

• Escherichia Coli 100%
• Dynamic Change 100%
• Structural Dynamics 100%
• Conformational Dynamics 100%
• Cyclic AMP Receptor Protein 100%
• DNA-binding Domain 60%
• Ligand-binding Domain 40%
• Fourier Transform Infrared Spectroscopy (FT-IR) 20%
• Activation Mechanism 20%
• Functional Domain 20%
• Dynamic Motion 20%
• Conformational Change 20%
• H-D Exchange 20%
• Cyclic GMP 20%
• Secondary Structure 20%
• Structural Composition 20%
• Amides 20%
• Gene number 20%
• Conformation Dynamics 20%
• In the Wild 20%
• Hydrogen-deuterium Exchange 20%
• Relaxation Effect 20%
• Secondary Structural Elements 20%
• Small DNA 20%
• Dynamic Conformations 20%
• Domain Shift 20%

Biochemistry, Genetics and Molecular Biology

• Dynamics 100%
• Cyclic Adenosine Monophosphate 100%
• Escherichia coli 100%
• Cyclic AMP Receptor 100%
• DNA-binding Domain 30%
• Wild Type 30%
• Binding Domain 20%
• Conformation 20%
• Conformational Change 10%
• Motion 10%
• Protein Secondary Structure 10%
• Hydrogen-Deuterium Exchange 10%
• Fourier Transform Infrared Spectroscopy 10%

Immunology and Microbiology

• Dynamics 100%
• Escherichia coli 100%
• DNA Binding 60%
• Wild Type 60%
• Conformation 40%
• Conformational Transition 20%
• Protein Secondary Structure 20%
• Fourier Transform Infrared Spectroscopy 20%
• Motion 20%