Functional roles of loops 3 and 4 in the cyclic nucleotide binding domain of cyclic AMP receptor protein from Escherichia coli

Keyphrases

• Escherichia Coli 100%
• Functional Role 100%
• Cyclic AMP Receptor Protein 100%
• Cyclic nucleotide-binding Domain 100%
• Tertiary Structure 50%
• Cyclic Adenosine Monophosphate (cAMP) 50%
• CAMP Receptor Protein 50%
• Quaternary Structure 50%
• Double mutant 50%
• Secondary Structure 50%
• Insertion mutation 50%
• Deletion mutation 50%
• Common Mechanisms 50%
• Binding Affinity 50%
• Sequence Difference 50%
• Intramolecular Communication 50%
• Regulatory Subunit 50%
• Cyclic nucleotide-gated Channel 50%
• Tuning Function 50%
• Functional Data 50%
• Protein Structural Motifs 50%
• Cyclic AMP-dependent Protein Kinase 50%
• Ligand Binding Affinity 50%

Biochemistry, Genetics and Molecular Biology

• Cyclic Adenosine Monophosphate 100%
• Escherichia coli 100%
• Cyclic AMP Receptor 100%
• Cyclic Nucleotide-Binding Domain 100%
• Binding Affinity 50%
• Eicosanoid Receptor 25%
• Tertiary Structure 25%
• Ligand Binding 25%
• Protein Quaternary Structure 25%
• Protein Secondary Structure 25%
• Protein Kinase A 25%
• Indel 25%
• Cyclic Nucleotide-Gated Ion Channel 25%
• Protein Structural Motifs 25%