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A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis

Nature volume 181, pages 662–666 (1958)Cite this article

MYOGLOBIN is a typical globular protein, and is found in many animal cells. Like haemoglobin, it combines reversibly with molecular oxygen; but whereas the role of haemoglobin is to transport oxygen in the blood stream, that of myoglobin is to store it temporarily within the cells (a function particularly important in diving animals such as whales, seals and penguins, the dark red tissues of which contain large amounts of myoglobin, and which have been our principal sources of the protein). Both molecules include a non-protein moiety, consisting of an iron-porphyrin complex known as the haem group, and it is this group which actually combines with oxygen; haemoglobin, with a molecular weight of 67,000, contains four haem groups, whereas myoglobin has only one. This, together with about 152 amino-acid residues, makes up a molecular weight of 17,000, so that myoglobin is one of the smaller proteins. Its small size was one of the main reasons for our choice of myoglobin as a subject for X-ray analysis.

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  1. Medical Research Council Unit for Molecular Biology, Cavendish Laboratory, Cambridge https://www.nature.com/nature

    J. C. Kendrew,  G. Bodo,  H. M. Dintzis,  R. G. Parrish &  H. Wyckoff

  2. Davy Faraday Laboratory, The Royal Institution, London https://www.nature.com/nature

    D. C. Phillips

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  1. J. C. Kendrew
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  2. G. Bodo
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  3. H. M. Dintzis
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Kendrew, J.C., Bodo, G., Dintzis, H. et al. A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis. Nature 181, 662–666 (1958). https://doi.org/10.1038/181662a0

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