Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe

Medicine & Life Sciences

• N-terminal monoferrictransferrin 100%
• Histidine 49%
• Iron 37%
• Ligands 31%
• Mutation 24%
• Carbonates 17%
• Transferrin 8%
• lysyllysine 7%
• Biochemistry 7%
• Iron-Binding Proteins 6%
• Binding Sites 6%
• Kinetics 5%
• Protein Stability 4%
• Anions 4%
• Ligation 3%
• Glutamic Acid 3%
• Metals 3%
• Carrier Proteins 3%
• Oxygen 2%
• Amino Acids 2%
• Serum 1%
• Proteins 1%

Chemical Compounds

• Histidine 42%
• Mutation 37%
• Carbonate 20%
• Ligand 19%
• Biochemistry 16%
• Glu-Ala 14%
• Glutamate Residue 12%
• Protein 11%
• Histidine Residue 10%
• Binding Site 6%
• Substitution Reaction 5%
• Anion 5%
• Dioxygen 4%
• Reduction 4%
• Metal 3%
• Time 3%
• Acid 3%