A possible allosteric communication pathway identified through a resonance raman study of four β337 mutants of human hemoglobin A

Chemical Compounds

• Hemoglobin 62%
• Heme 62%
• Communication 61%
• Resonance 53%
• Strain 35%
• Tetramer 33%
• Biochemistry 30%
• Environment 28%
• Interface State 25%
• Resonance Raman Spectroscopy 20%
• Quaternary Structure 20%
• Plastic Property 19%
• Effector 18%
• Tertiary Structure 17%
• Histidine 16%
• Tryptophan 15%
• Photolysis 14%
• Mutation 14%
• X-Ray Crystallography 13%
• Protein 13%
• Displacement 13%
• Raman Spectrum 13%
• Dissociation 12%
• Binding Site 11%
• Force 11%
• Hydrogen Bond 10%
• X-Ray 10%
• Dioxygen 8%

Medicine & Life Sciences

• Hemoglobin A 100%
• Heme 74%
• Communication 50%
• Ligands 31%
• Biochemistry 20%
• Iron 18%
• Hemoglobins 18%
• Photolysis 15%
• X Ray Crystallography 15%
• Raman Spectrum Analysis 14%
• Hydrogen Bonding 13%
• Histidine 12%
• Mutant Proteins 12%
• Tryptophan 11%
• Carbon Monoxide 11%
• Lasers 9%
• X-Rays 8%
• Binding Sites 8%
• Oxygen 8%
• Mutation 6%
• Proteins 4%