Polypeptide chain configurations in crystalline proteins

  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},
  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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  • Medicine, Chemistry
  • International journal of peptide and protein research
  • 1972
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  • Chemistry
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2003
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