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Is cooperative oxygen binding by hemoglobin really understood?

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Abstract

The enormous success of structural biology challenges the physical scientist. Can biophysical studies provide a truly deeper understanding of how a protein works than can be obtained from staticstructures and qualitative analysis of biochemical data? We address this question in a case study by presenting the key concepts and experimental results that have led to our current understanding of cooperative oxygen binding by hemoglobin, the paradigm of structure-function relations in multi-subunit proteins. We conclude that the underlying simplicity of the two-state allosteric mechanism could not have been demonstrated without novel physical experiments and a rigorous quantitative analysis.

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Authors and Affiliations

  1. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Building 5, 20892-0520, Bethesda, Maryland, U.S.A.

    William A. Eaton, Eric R. Henry & James Hofrichter

  2. Dipartimento di Biochimica e Biologia Molecolare, Università degli Studi di Parma, Parco Area delle Scienze, 23/A, 43100, Parma

    Andrea Mozzarelli

Authors
  1. William A. Eaton
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  2. Eric R. Henry
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  3. James Hofrichter
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  4. Andrea Mozzarelli
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Correspondence to William A. Eaton.

Additional information

Reprinted from Nature Structural Biology, vol. 6, W.A. Eaton, E.R. Henry, J. Hofrichter, and A. Mozzarelli,Is cooperative oxygen binding by hemoglobin really understood?, pp. 351–358, Copyright (1999), with permission from Nature Publishing Group.

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Eaton, W.A., Henry, E.R., Hofrichter, J. et al. Is cooperative oxygen binding by hemoglobin really understood?. Rend. Fis. Acc. Lincei 17, 147–162 (2006). https://doi.org/10.1007/BF02904506

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