Allosteric transitions in hemoglobin revisited

• Published in: Biochimica et biophysica acta. General subjects Vol. 1864; no. 2; p. 129335
• Main Author: Shibayama, Naoya
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2020
• Subjects: Allosteric regulation; Allostery; Conformational change; Hemoglobin; humans; ligands; oxygen; Protein function; structure-activity relationships; X-ray crystallography; XL[α(Fe)β(Ni)]2; HL; nmax; FL; Conformational change; PDB; X-ray crystallography; IHP; R; XL[α(Ni)β(Fe)]2; T; Protein function; Hemoglobin; Pi; R2; Allostery; RMSD; P50; BZF; XL[α(Fe-CO)β(Ni)][α(Ni)β(Fe-CO)]; XL[α(Fe)β(Ni)][α(Ni)β(Fe)]; RR2; PEG; Allosteric regulation; BPG; XL[α(Fe)β(Fe)][α(Ni)β(Ni)]; TR; Ki

Human hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model without intermediates offers a simple qualitative description of the allosteric behavior of hemoglobin, as presented in textbooks. However, ther...