Structure of the Synthetic Polypeptide Poly-γ-methyl-L-glutamate

@article{Yakel1952StructureOT,
  title={Structure of the Synthetic Polypeptide Poly-$\gamma$-methyl-L-glutamate},
  author={Harry L. Yakel and Linus Carl Pauling and Robert B. Corey},
  journal={Nature},
  year={1952},
  volume={169},
  pages={920-920}
}
WE have made a check on the assignment of the α-helix with eighteen residues in five turns to poly-γ-methyl-L-glutamate1 by preparing and interpreting X-ray photographs of a sample of the material. The results obtained not only support the assignment, but also indicate that the β-carbon atoms are in position 2 rather than in position 1 2. This is the same assignment of the β-carbon atoms as that made by Riley and Arndt3 for serum albumin, on the basis of their determination of the radial… 
12 Citations
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TLDR
Evidence that one of the helical structures is assumed also by synthetic polypeptides is discussed, which is an important structural feature of hemoglobin and other globular proteins.
Evidence for the Pauling–Corey α-Helix in Synthetic Polypeptides
TLDR
It is shown here that the correspondence extends over the whole of the diffraction pattern of the synthetic polypeptide poly-γ-methyl-L-glutamate, so readily explained on this basis as to leave little doubt that the Pauling–Corey α-helix2, or some close approximation to it, exists in this polypeptic.
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    Proceedings of the National Academy of Sciences of the United States of America
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TLDR
The discovery of two helical configurations of the polypeptide chain that satisfy the conditions for diffraction of x-rays in the equatorial direction are reported.