Published May 1, 1951
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Journal Article
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The pleated sheet, a new layer configuration of polypeptide chains
- Creators
- Pauling, Linus
- Corey, Robert B.
Chicago
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Abstract
For many years it has been assumed that in silk fibroin, stretched hair and muscle, and other proteins with the β-keratin structure the polypeptide chains are extended to nearly their maximum length, about 3.6 A per residue, and during the last decade it has been assumed also that the chains form lateral hydrogen bonds with adjacent chains, which have the opposite orientation. A hydrogen-bonded layer of this sort is represented diagrammatically in figure 1.(1-4)
Additional Information
© 1951 by the National Academy of Sciences. Communicated March 31, 1951. This investigation was aided by grants from The Rockefeller Foundation, The National Foundation for Infantile Paralysis, and The United States Public Health Service. Gates and Crellin Laboratories of Chemistry, Contribution No. 1552.Files
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- 8084
- Resolver ID
- CaltechAUTHORS:PAUpnas51e
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