Literature DB >> 262394

A simple tension-displacement model for hemoglobin cooperativity.

L J Groome, J C Telotte.   

Abstract

Based on the Perutz view of hemoglobin cooperativity and the methodology of statistical physics, a molecular model for heme-heme interactions is proposed. The motion of the iron atom with respect to the heme plane is assumed to be the important feature of the oxygenation step, and results in an expression for hemoglobin saturation as an explicit function of the internal tension of the hemoglobin molecule. Closure of the equation is obtained with the assumption of linearity between the internal tension and the displacement of the iron atom above the heme plane. All model parameters are physically realizable and are characteristic of the hemoglobin molecule. Finally, the model is capable of discriminating between positive and negative cooperativity.

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Year:  1979        PMID: 262394      PMCID: PMC1328473          DOI: 10.1016/s0006-3495(79)85300-x

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  5 in total

1.  Nature of haem-haem interaction.

Authors:  M F Perutz
Journal:  Nature       Date:  1972-06-30       Impact factor: 49.962

2.  Diagnostic uses of the Hill (Logit and Nernst) plots.

Authors:  A Cornish-Bowden; D E Koshland
Journal:  J Mol Biol       Date:  1975-06-25       Impact factor: 5.469

3.  The combining power of hemoglobin for alkyl isocyanides, and the nature of the heme-heme interactions in hemoglobin.

Authors:  R C C ST GEORGE; L PAULING
Journal:  Science       Date:  1951-12-14       Impact factor: 47.728

4.  Relation between structure, co-operativity and spectra in a model of hemoglobin action.

Authors:  J J Hopfield
Journal:  J Mol Biol       Date:  1973-06-25       Impact factor: 5.469

5.  Stereochemistry of cooperative effects in haemoglobin.

Authors:  M F Perutz
Journal:  Nature       Date:  1970-11-21       Impact factor: 49.962

  5 in total

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