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

@article{Kendrew1958ATM,
  title={A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis},
  author={John Cowdery Kendrew and Gerhard Prof Dr Bodo and Howard M. Dintzis and Rob G. Parrish and Harold W. Wyckoff and David C. Phillips},
  journal={Nature},
  year={1958},
  volume={181},
  pages={662-666}
}
Myoglobin is a typical globular protein, and is found in many animal cells. Like hæmoglobin, it combines reversibly with molecular oxygen; but whereas the role of hæmoglobin is to transport oxygen in the blood stream, that of myoglobin is to store it temporarily within the cells (a funcJon parJcularly important in diving animals such as whales, seals and penguins, the dark red Jssues of which contain large amounts of myoglobin, and which have been our principal sources of the protein). Both… 
Structural and oxygen binding properties of dimeric horse myoglobin.
TLDR
It is found that dimeric metMb exhibits a domain-swapped structure with two extended α-helices, and results show that domain swapping may be a new tool for protein engineering.
The crystal structure of myoglobin, V. A low-resolution three-dimensional Fourier synthesis of sperm-whale myoglobin crystals
The study of type A crystals of sperm-whale has now been extended to three dimensions by using the method of isomorphous replacement to determine the phases of all the general X-ray reflexions having
Structural stability of myoglobin and glycomyoglobin: a comparative molecular dynamics simulation study
TLDR
The simple addition of a covalently bound glucose is suggested to exert its stabilizing effect via increased contacts with surrounding water molecules, as well as a different pattern of interactions with neighbor residues.
Snapshots of a protein quake
TLDR
Three-dimensional snapshots of structural changes in myoglobin—low-amplitude collective motions that rapidly spread throughout the protein—that occur during the first few picoseconds after the CO photodissociation are provided.
HEMOGLOBIN AND MYOGLOBIN.
Electronic control of ligand-binding preference of a myoglobin mutant.
TLDR
The L29F mutant of sperm whale myoglobin, where the leucine 29 residue was replaced by phenylalanine (Phe), was shown to exhibit remarkably high affinity to oxygen (O2), and the tuning of the intrinsic heme Fe reactivity through the heme electronic structure in functional regulation of Mb was highlighted.
Molecular cloning and 3D structure prediction of myoglobin and cytoglobin in Eurasian Tree Sparrow Passer montanus
TLDR
The results show that the amino acid sequences and three-dimensional structures of Mb and Cygb are highly conserved in vertebrates, as well as the potential mechanisms of oxygen utilization pathways in vertebrate species.
...
1
2
3
4
5
...

References

SHOWING 1-8 OF 8 REFERENCES
The crystal structure of myoglobin III. Sperm-whale myoglobin
  • J. Kendrew, R. Parrish
  • Chemistry
    Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences
  • 1957
Myoglobin of Physeter catodon (sperm whale) forms monoclinic crystals with space group P21 (type A) in ammonium sulphate, and orthorhombic crystals with space group P21 21 21 (type B) in phosphate.
The structure of haemoglobin - IV. Sign determination by the isomorphous replacement method
Native horse haemoglobin contains free sulphydryl groups and forms crystalline compounds with para-mercuribenzoate groups and with silver ions. Crystals in which two of the four available SH groups
The structure of haemoglobin - VI. Fourier projections on the 010 plane
  • W. Bragg, M. Perutz
  • Chemistry
    Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences
  • 1954
In the preceding papers the molecular Fourier transform was measured as a continuous function of c* along nine lines of constant h in the plane of k = 0. Fourier inversion of this transform gives an
Electron Spin Resonance in Myoglobin and Hæmoglobin: Orientation of the Hæm Group in Myoglobin and its Relation to the Polypeptide Chain Direction
Electron Spin Resonance in Myoglobin and Haemoglobin: Orientation of the Haem Group in Myoglobin and its Relation to the Polypeptide Chain Direction
Isomorphous replacement and phase determination in non‐centrosymmetric space groups
below, for the a tom 09 is a t y = 1⁄4 , and it would therefore lie over a t rough if the second layer were undisplaced with respect to the first. In these circumstances the h06 reflexions would