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ABSTRACT ACCORDING to the classical researches of Fischer and others, proteins would appear to be essentially polypeptides, giant molecules formed by the repeated condensation of
a-amino-acids. This concept leads naturally to the idea of long chain-molecules like that of cellulose, the structure of which was worked out some years ago by a particularly happy
combination of chemical and X-ray methods1. Similar methods applied to one of the simplest proteins, fibroin, the fibre substance of natural silk, show that, for silk at least, the
hypothesis is substantially correct1; that, in fact, this fibre is a kind of molecular yarn or sliver built up by chain-like molecules, fully-extended polypeptides, lying roughly parallel to
the fibre axis. The approximate dimensions of these chain-molecules may be predicted from atomic data already available, and they are found to fit in well with the results of X-ray
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support REFERENCES * K. H. Meyer and H. Mark, ” _Der Aufbau der hochpolymeren organischen Naturstoffe_”, 1930. Google Scholar * W. T. Astbury, _J. Soc. Chem. Ind._, 49, 441 (1930). _J.
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AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Textile Physics Laboratory, University of Leeds, W. T. Astbury Authors * W. T. Astbury View author publications You can also search for this
author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Astbury, W. X-Ray Studies of Protein Structure. _Nature_ 137, 803–805
(1936). https://doi.org/10.1038/137803a0 Download citation * Issue Date: 16 May 1936 * DOI: https://doi.org/10.1038/137803a0 SHARE THIS ARTICLE Anyone you share the following link with will
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