Biochemistry & Analytical Biochemistry

Department of Chemistry and Biochemistry, University of California, San Diego, USA

Publications

• Review Article   
  De-Constructing the ^TState/^RState Structure Change of Human Hemoglobin
  Author(s): Francis Knowles* and Douglas Magde
  
  The dimensionless equilibrium constant for the allosteric structure change is shown to be comprised of: (i) An endothermic change in structure, from Tstate to Rstate, of 24.3 kJ/mol; (ii) Exothermic conversion of Tstate TαO2- chains to Rstate RαO2-chains of-13.8 kJ/mol; (iii) Exothermic binding of BPG by R-states. Equation (1) defines the component steps whereby the Tstate structure is converted to the Rstate structure. ΔG°(R(Hb4), BPG) describes the endothermic decomposition of the binary complex, THb4/BPG into RHb4 and BPG, equal to +33.7 kJ/mol (DeBruin et al. (1973). J. Biol. Chem. 248, 2774-2777). ΔG° of the equilibrium constant for ΔG° (KΔ) and ? &.. View more»
  

  DOI: 10.35248/2161-1009.23.12.479

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