The amino acid sequence of human myoglobin and its minor fractions

The complete amino acid sequence of human skeletal myoglobin is described. That of heart myoglobin is found by homology to be the same. When myoglobin is prepared some minor fractions may be obtained besides the main component. They are shown to be artefacts arising from deamidations. The likely three-dimensional structure of human myoglobin is discussed, taking that of sperm-whale myoglobin as a reference. Human myoglobin is compared with the α - and β -chains of human haemoglobin. There is a noteworthy similarity of internal residues and haem contacts, but little resemblance of sites where the haemoglobin chains form dimeric and tetrameric contacts, when they become subunits of the haemoglobin molecule.

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The covalent and three-dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)41841-3 ◽

1975 ◽

Vol 250 (4) ◽

pp. 1503-1512

Author(s):

B A Cunningham ◽

J L Wang ◽

M J Waxdal ◽

G M Edelman

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Concanavalin A ◽

Cyanogen Bromide ◽

Three Dimensional ◽

Dimensional Structure ◽

Three Dimensional Structure ◽

Cyanogen Bromide Fragment

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The Amino-Acid Sequence of Sperm Whale Myoglobin: Chemical Studies

Nature ◽

10.1038/190663a0 ◽

1961 ◽

Vol 190 (4777) ◽

pp. 663-665 ◽

Cited By ~ 92

Author(s):

A. B. EDMUNDSON ◽

C. H. W. HIRS

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Sperm Whale ◽

Chemical Studies ◽

Sperm Whale Myoglobin

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The structure of haemoglobin. IX. A three-dimensional Fourier synthesis at 5.5 Å resolution: description of the structure

Proceedings of the Royal Society of London Series A - Mathematical and Physical Sciences ◽

10.1098/rspa.1962.0002 ◽

1962 ◽

Vol 265 (1321) ◽

pp. 161-187 ◽

Cited By ~ 70

Keyword(s):

Tertiary Structure ◽

Three Dimensional ◽

Sperm Whale ◽

Anomalous Scattering ◽

Fourier Synthesis ◽

Human Haemoglobin ◽

Contour Maps ◽

To Come ◽

Polypeptide Chains ◽

Sperm Whale Myoglobin

The electron density distribution in the unit cell is calculated at intervals of approximately 2Å and plotted in a series of sections parallel to (010). The contour maps show that haemoglobin consists of four subunits in a tetrahedral array. The subunits are identical in pairs in accordance with the twofold symmetry of the molecule. The two pairs are very similar in structure, and the members of each pair closely resemble the molecule of sperm-whale myoglobin. The four haem groups lie in separate pockets at the surface of the molecule. The positions of the iron atoms are confirmed by comparison of observed and calculated anomalous scattering effects, which also serve to determine the absolute configuration of the molecule. The four subunits found by X-ray analysis correspond to the four polypeptide chains into which haemoglobin can be divided by chemical methods. In horse haemoglobin the amino acid sequence within these chains is still partly unknown, but in human haemoglobin it has already been determined. Comparison of this sequence with the tertiary structure of the chains as now revealed in horse haemoglobin and with the atomic model of sperm-whale myoglobin recently obtained by Kendrew and his collaborators shows many interesting relations. Prolines appear to come where the chains turn corners or where their configuration is known to be non-helical. On the other hand, the chains also have corners which contain no proline. Certain residues appear to be structurally vital, because they appear in identical positions in myoglobin and in the two chains of haemoglobin, while in other parts of the molecule a wide variety of different side-chains appears to be allowed.

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[35] Three-dimensional profiles for measuring compatibility of amino acid sequence with three-dimensional structure

Methods in Enzymology - Computer Methods for Macromolecular Sequence Analysis ◽

10.1016/s0076-6879(96)66037-6 ◽

1996 ◽

pp. 598-616 ◽

Cited By ~ 8

Author(s):

James U. Bowie ◽

Kam Zhang ◽

Matthias Wilmanns ◽

David Eisenberg

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Three Dimensional ◽

Dimensional Structure ◽

Three Dimensional Structure

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Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding?

Quarterly Reviews of Biophysics ◽

10.1017/s0033583500001724 ◽

1980 ◽

Vol 13 (3) ◽

pp. 339-386 ◽

Cited By ~ 155

Author(s):

O. B. Ptitsyn ◽

A. V. Finkelstein

Keyword(s):

Serine Proteases ◽

Protein Structures ◽

Three Dimensional ◽

Sperm Whale ◽

Globular Protein ◽

Dimensional Structure ◽

Evolutionary Divergence ◽

Functional Convergence ◽

Primary Structures ◽

Sperm Whale Myoglobin

(A) Evolutionary similarities of protein structures Two decades have passed from the time that the three dimensional structure of the first globular protein, sperm whale myoglobin, was decoded (Kendrew et al. 1960). Its structure, which now looks so simple and habitual, then seemed to be unusually complicated. The decoding of the subsequent proteins, lysozyme (Blake et al. 1965), ribonuclease (Kartha, Bello & Harker, 1967), chymotrypsin (Matthews et al. 1967), carboxypeptidase (Lipscomb et al. 1969) redoubled the feeling of amazement and even of some confusion before the extremely complicated, intricate and, above all, absolutely unlike protein structures. Some consolation against this background was the evident and far-reaching similarity between the three-dimensional structures of myoglobin and hemoglobin subunits (Perutz, Kendrew & Watson, 1965) and an analogous similarity between the structures of chymotrypsin and other serine proteases, elastase (Shotton & Watson, 1970) and trypsin (Stroud, Kay & Dickerson, 1972). However this similarity was easily explained by the far-reaching homology between the primary structures of myoglobin and hemoglobin and between the primary structures of serine proteases.

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