Exploring the RNase A scaffold to combine catalytic and antimicrobial activities. Structural characterization of RNase 3/1 chimeras

Keyphrases

• Ribonuclease 100%
• Structural Characterization 100%
• Chimera 100%
• Catalytic Activity 100%
• Antimicrobial Activity 100%
• RNase3 100%
• RNase1 42%
• Catalytic Efficiency 28%
• Structure Function 14%
• X-ray Crystallography 14%
• Antimicrobial Resistance 14%
• 3D Structure 14%
• Pharmacophore 14%
• Protein-based 14%
• Novel Protein 14%
• Ribonuclease Inhibitor 14%
• Chimeric Protein 14%
• Functional Regions 14%
• Dinucleotide 14%
• Antimicrobial Properties 14%
• Base Selectivity 14%
• RNase A Superfamily 14%
• Atomic Resolution 14%
• High Catalytic Activity 14%
• Alternative Therapy 14%
• Non-cytotoxic 14%
• Substrate Binding 14%
• C-terminal Region 14%
• Binding Cavity 14%
• Molecular Docking 14%
• Antipathogens 14%
• Antipathogenic Activity 14%
• Novel Antibiotics 14%
• Flexible Loop 14%
• Protein chimera 14%
• Active Site Conformation 14%
• Global Health Priorities 14%
• Anti-infective Therapy 14%

Biochemistry, Genetics and Molecular Biology

• Ribonuclease 100%
• Ribonuclease A 100%
• Antimicrobial Activity 100%
• Enzymatic Activity 20%
• Catalytic Efficiency 20%
• Conformation 10%
• Active Site 10%
• X-Ray Crystallography 10%
• Flexible Loop 10%
• Antibiotic Resistance 10%
• Cytotoxicity 10%
• C-Terminus 10%
• Ribonuclease Inhibitor 10%
• Pharmacophore 10%
• Docking (Molecular) 10%
• Chimeric Protein 10%