The human peripheral subunit-binding domain folds rapidly while overcoming repulsive Coulomb forces

Keyphrases

• Ligand-binding Domain 100%
• Coulomb Force 100%
• Protein Stability 40%
• Folding Kinetics 40%
• Positive Surface Charge 20%
• High Density 20%
• Protein Function 20%
• Ionic Strength 20%
• Protein Folding 20%
• Circular Dichroism 20%
• Native State 20%
• Debye 20%
• Catalytic Subunit 20%
• Protein Surface 20%
• Surface Charge Density 20%
• Enzyme Complex 20%
• Positive Charge 20%
• Carbohydrate Metabolism 20%
• Surface Charge Distribution 20%
• Solution Ionic Strength 20%
• Protein Evolution 20%
• Solvent Conditions 20%
• Tryptophan Fluorescence 20%
• Marginally Stable 20%
• Folding Thermodynamics 20%
• Prosthetic Group 20%
• Two-state Transition 20%
• Stability Kinetics 20%

Immunology and Microbiology

• Ionic Strength 100%
• Surface Charge 100%
• Protein Stability 100%
• Surface Property 50%
• Solution and Solubility 50%
• Protein Function 50%
• Protein Folding 50%
• Enzyme Active Site 50%
• Carbohydrate Metabolism 50%
• Static Electricity 50%

Biochemistry, Genetics and Molecular Biology

• Binding Domain 100%
• Surface Charge 40%
• Ionic Strength 40%
• Solution and Solubility 20%
• Membrane Protein 20%
• Transmembrane Protein 20%
• Static Electricity 20%
• Protein Function 20%
• Protein Stability 20%
• Protein Folding 20%
• Enzyme Active Site 20%
• Circular Dichroism 20%
• Tryptophan 20%
• Multienzyme Complex 20%
• Carbohydrate Metabolism 20%
• Folding Kinetics 20%