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The pleated sheet, a new layer configuration of polypeptide chains

Pauling, Linus and Corey, Robert B. (1951) The pleated sheet, a new layer configuration of polypeptide chains. Proceedings of the National Academy of Sciences of the United States of America, 37 (5). pp. 251-256. ISSN 0027-8424.

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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)

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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.
Issue or Number:5
Record Number:CaltechAUTHORS:PAUpnas51e
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:8084
Deposited By: Tony Diaz
Deposited On:30 Jul 2007
Last Modified:02 Oct 2019 23:48

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