Literature DB >> 429325

Thermodynamic studies on the oxygenation and subunit association of human hemoglobin. Temperature dependence of the linkage between dimer-tetramer association and oxygenation state.

F C Mills, G K Ackers.   

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Year:  1979        PMID: 429325

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


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  7 in total

1.  Resonance Raman spectra of photodissociated hemoglobins: implications on cooperative mechanisms.

Authors:  D L Rousseau; M R Ondrias
Journal:  Biophys J       Date:  1985-04       Impact factor: 4.033

2.  Linkage between ligand binding and the dimer-tetramer equilibrium in the Monod-Wyman-Changeux model of hemoglobin.

Authors:  S J Edelstein; J T Edsall
Journal:  Proc Natl Acad Sci U S A       Date:  1986-06       Impact factor: 11.205

3.  Allosteric interpretation of the measurement of cooperative free energy in cyanomethemoglobin.

Authors:  F A Ferrone
Journal:  Proc Natl Acad Sci U S A       Date:  1986-09       Impact factor: 11.205

4.  The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids.

Authors:  Y Huang; M L Doyle; G K Ackers
Journal:  Biophys J       Date:  1996-10       Impact factor: 4.033

5.  Energetics of subunit assembly and ligand binding in human hemoglobin.

Authors:  G K Ackers
Journal:  Biophys J       Date:  1980-10       Impact factor: 4.033

6.  Ligand binding and self-association of proteins.

Authors:  R F Steiner
Journal:  Mol Cell Biochem       Date:  1980-05-28       Impact factor: 3.396

7.  Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin.

Authors:  S W Englander; J J Englander; R E McKinnie; G K Ackers; G J Turner; J A Westrick; S J Gill
Journal:  Science       Date:  1992-06-19       Impact factor: 47.728

  7 in total

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