Dimerization of coronavirus nsp9 with diverse modes enhances its nucleic acid binding affinity

Keyphrases

• Coronavirus 100%
• Dimerization 100%
• Binding Affinity 100%
• Nucleic Acid Binding 100%
• Non-structural Protein 100%
• Porcine deltacoronavirus (PDCoV) 33%
• Porcine Epidemic Diarrhea Virus 33%
• Amino Acids 6%
• Economic Stability 6%
• Health Threat 6%
• Dimer Interface 6%
• Global Health 6%
• RNA-binding Protein 6%
• Electrophoretic Mobility Shift Assay 6%
• Analytical Ultracentrifugation 6%
• Size Exclusion Chromatography 6%
• Disulfide Bond 6%
• Coronavirus Replication 6%
• Microscale Thermophoresis 6%
• Global Economics 6%

Biochemistry, Genetics and Molecular Biology

• Dimerization 100%
• Nucleic Acid Binding 100%
• Binding Affinity 100%
• Coronavirinae 100%
• Porcine Epidemic Diarrhea Virus 55%
• Wild Type 33%
• Solution and Solubility 11%
• Amino Acids 11%
• Crystal Structure 11%
• RNA-binding Protein 11%
• Electrophoretic Mobility Shift Assay 11%
• N-Terminus 11%
• Size-Exclusion Chromatography 11%
• Disulfide Bond 11%
• Ultracentrifugation 11%

Immunology and Microbiology

• Coronavirinae 100%
• Binding Affinity 100%
• Dimerization 100%
• Porcine Epidemic Diarrhea Virus 55%
• Wild Type 33%
• Size Exclusion Chromatography 11%
• Protein RNA Binding 11%
• Solution and Solubility 11%
• Amino Terminal Sequence 11%
• Gel Mobility Shift Assay 11%
• Crystal Structure 11%
• Ultracentrifugation 11%
• Coronavirus 11%
• Disulfide Bond 11%
• Amino Acid 11%