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Three Dimensional Structure of Haemoglobin Rainier

Nature New Biology volume 230, pages 261–264 (1971)Cite this article

Abstract

The difference electron density map of deoxyhaemoglobin Rainier (α2β2145Tyr→Cys) shows that the cysteine introduced by the mutation forms a disulphide bridge with the reactive cysteine, F9(93)β, of the same β-chain. The resulting structural distortions affect the C-terminus of the β-chain, thereby inhibiting part of the alkaline Bohr effect and haem–haem interaction.

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Author notes

  1. J. GREER

    Present address: Department of Molecular Biophysics, Yale University, New Haven, Connecticut, 06520

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  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge

    J. GREER & M. F. PERUTZ

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  1. J. GREER
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  2. M. F. PERUTZ
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GREER, J., PERUTZ, M. Three Dimensional Structure of Haemoglobin Rainier. Nature New Biology 230, 261–264 (1971). https://doi.org/10.1038/newbio230261a0

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