Nuclear Magnetic Resonance Studies of Bovine Carbonic Anhydrase. Binding of Sulfonamides to the Zinc Enzyme

Keyphrases

• Active Sites 50%
• Aromatic Ring 50%
• Aromatics 50%
• Binding Constant 50%
• Binding Mode 50%
• Bovine Carbonic Anhydrase 100%
• Broadening Effect 50%
• Chemical Shift 50%
• Dipolar Relaxation 100%
• Dissociation Rate Constant 50%
• Enzymatic Activity 50%
• Enzyme-inhibitor Complex 50%
• Frequency Dependence 50%
• Line Broadening 50%
• Magnetic Resonance Techniques 100%
• Methyl Groups 50%
• Methyl Protons 50%
• Nuclear Magnetic Resonance 100%
• Nuclear Magnetic Resonance Technique 50%
• Protein Molecules 50%
• Proton 100%
• Proton-proton Interactions 50%
• Relaxation Mechanism 50%
• Resonance Line 50%
• Rotational Motion 50%
• Specific Binding 50%
• Sulfonamide Antibiotics 100%
• Sulfonamides 100%
• Two-frequency 50%
• Whole Protein 50%
• Zinc 50%
• Zinc Enzyme 100%

Biochemistry, Genetics and Molecular Biology

• Active Site 33%
• Binding Affinity 33%
• Carbonic Anhydrase 100%
• Dissociation Rate Constant 33%
• Enzyme Activity 33%
• Enzyme Inhibitor Complex 33%
• Motion 33%
• Sulfonamide 100%
• Zinc Enzymes 100%