Influence of an Intrinsically Disordered Region on Protein Domains Revealed by NMR-Based Electrostatic Potential Measurements

Keyphrases

• DNA-binding Domain 100%
• Protein Domain 100%
• Nuclear Magnetic Resonance 100%
• Intrinsically Disordered Region 100%
• Electrostatic Potential 100%
• Potential Measure 100%
• HMGB1 Protein 75%
• DNA-binding Proteins 50%
• Local Electrostatics 50%
• Electrostatic Properties 50%
• Protein-DNA Complex 25%
• Counterion 25%
• NMR Spectroscopy 25%
• Glutamate 25%
• Dissociation 25%
• Positively Charged 25%
• Charged Residue 25%
• Aspartate 25%
• Folded Domains 25%
• Electrostatic Interaction 25%
• High Mobility Group Box 1 (HMGB1) 25%
• Human Proteins 25%
• Molecular Behavior 25%

Neuroscience

• DNA Binding 100%
• Nuclear Magnetic Resonance 100%
• Protein Tertiary Structure 100%
• High Mobility Group B1 Protein 75%
• RNA-binding Protein 50%
• Behavior (Neuroscience) 25%
• Glutamic Acid 25%
• Aspartic Acid 25%
• Nuclear Magnetic Resonance Spectroscopy 25%
• DNA Protein Complex 25%
• HMGB1 25%

Biochemistry, Genetics and Molecular Biology

• DNA-binding Domain 100%
• HMGB1 100%
• Protein Tertiary Structure 100%
• DNA RNA Hybridization 50%
• RNA-binding Protein 50%
• DNA Protein Complex 25%
• Static Electricity 25%
• Glutamic Acid 25%
• Aspartic Acid 25%
• Nuclear Magnetic Resonance Spectroscopy 25%