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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.

In describing a protein it is now common to distinguish the primary, secondary and tertiary structures. The primary structure is simply the order, or sequence, of the amino-acid residues along the polypeptide chains. This was first determined by Sanger using chemical techniques for the protein insulin1, and has since been elucidated for a number of peptides and, in part, for one or two other small proteins. The secondary structure is the type of folding, coiling or puckering adopted by the polypeptide chain: the α-helix and the pleated sheet are examples. Secondary structure has been assigned in broad outline to a number of fibrous proteins such as silk, keratin and collagen; but we are ignorant of the nature of the secondary structure of any globular protein. True, there is suggestive evidence, though as yet no proof, that α-helices occur in globular proteins, to an extent which is difficult to gauge quantitatively in any particular case. The tertiary structure is the way in which the folded or coiled polypeptide chains are disposed to form the protein molecule as a three-dimensional object, in space. The chemical and physical properties of a protein cannot be fully interpreted until all three levels of structure are understood, for these properties depend on the spatial relationships between the amino-acids, and these in turn depend on the tertiary and secondary structures as much as on the primary.

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Authors and Affiliations

  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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