Polypeptide chain configurations in crystalline proteins

@article{Bragg1950PolypeptideCC,
  title={Polypeptide chain configurations in crystalline proteins},
  author={W. Bragg and J. Kendrew and M. Perutz},
  journal={Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences},
  year={1950},
  volume={203},
  pages={321 - 357}
}
  • W. Bragg, J. Kendrew, M. Perutz
  • Published 1950
  • Chemistry
  • Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences
Astbury’s studies of α-keratin, and X-ray studies of crystalline haemoglobin and myoglobin by Perutz and Kendrew, agree in indicating some form of folded polypeptide chain which has a repeat distance of about 5·1 Å, with three amino-acid residues per repeat. In this paper a systematic survey has been made of chain models which conform to established bond lengths and angles, and which are held in a folded form by N—H—O bonds. After excluding the models which depart widely from the observed… Expand
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In an interesting recent paper by Astbury, Dalgleish, Darmon and Sutherland the properties of some synthetic polypeptides and natural proteins have been discussed, both from the point of view of X-ray diffraction and infra-red absorption. Expand
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THE quest for the structure of the α-form of members of the keratin–myosin–epidermis–fibrinogen group of fibrous proteins has recently been encouraged by the discovery among X-ray photographs ofExpand
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