Negative Cooperativity in the Binding of Nucleotides to Escherichia coli Replicative Helicase DnaB Protein. Interactions with Fluorescent Nucleotide Analogs

Keyphrases

• Escherichia Coli 100%
• Replicative Helicase 100%
• Nucleoside Analogues 100%
• Negative Cooperativity 100%
• Diphosphate 100%
• Fluorescent nucleosides 100%
• Nucleotide Binding 75%
• Adenosine Triphosphate 75%
• Adenosine Diphosphate 75%
• Protein-like Fluorescence 75%
• DNA Helicase 50%
• Hexamer 50%
• Binding Isotherm 50%
• Nucleotide Binding Site 50%
• Binding Phase 50%
• Adenosine 5′-monophosphate 25%
• Binding Site 25%
• Binding Mechanism 25%
• Fluorescence Titration 25%
• Titration Curve 25%
• Low-affinity Binding Sites 25%
• High-affinity Binding 25%
• Intrinsic Binding Constant 25%
• Intrinsic Properties 25%
• Cooperativity 25%
• Statistical Thermodynamic Model 25%
• Phosphate Group 25%
• Binding Parameters 25%
• Interaction Parameter 25%
• High Temperature 25%
• Fluorescence Quenching 25%
• Rigorous Method 25%
• Modifying Groups 25%
• Empirical Function 25%
• Exact Representation 25%
• Hexagon 25%
• Quenching Constant 25%
• High Heterogeneity 25%

Biochemistry, Genetics and Molecular Biology

• Escherichia coli 100%
• Helicase 100%
• Adenosine Diphosphate 100%
• DnaB Helicase 100%
• Cooperation 100%
• Pyrophosphate 66%
• Binding Affinity 50%
• Adenosine Triphosphate 50%
• Nucleotide Binding Site 33%
• Cyclic Adenosine Monophosphate 16%
• Binding Site 16%
• Quenching (Fluorescence) 16%