Abstract
THE α-helix was proposed by Pauling et al.1 as a stable configuration of the polypeptide chain, and considerable support for this view was obtained from the X-ray diffraction patterns yielded by naturally occurring and synthetic polypeptides2,3. The diameter of the α-helix was estimated to be about 10 Å and includes the contribution of the side-chains as well as the main-chains of the protein4. Direct proof of the existence of α-helices in the globular protein myoglobin was obtained by Fourier synthesis methods5, and there is evidence suggesting that the α-group of fibrous proteins contains rope—or cable-like assemblies of distorted α-helices4,6.
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DOBB, M. α-Helix in Fibrous Proteins. Nature 207, 293 (1965). https://doi.org/10.1038/207293a0
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DOI: https://doi.org/10.1038/207293a0
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