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Stable Configurations of Polypeptide Chains

Pauling, L. and Corey, R. B. (1953) Stable Configurations of Polypeptide Chains. Proceedings of the Royal Society of London. Series B, Biological Sciences, 141 (902). pp. 21-33. ISSN 0962-8452. doi:10.1098/rspb.1953.0012.

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Several configurations of polypeptide chains involving planar amide groups with the dimensions found by experiment for simple substances, and hydrogen bonds between the NH groups and the carbonyl oxygen atoms, have been discovered. One of these structures, the α-helix, with about 3·7 amino-acid residues per turn of the helix, has been assigned to synthetic polypeptides and proteins that give X-ray diagrams of the α-keratin type. The evidence supporting this assignment is reviewed. Other configurations of polypeptide chains, including the γ-helix, three pleated-sheet structures, and the three-chain helical structure proposed for collagen, are described, and evidence bearing on their possible presence in proteins is discussed.

Item Type:Article
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Additional Information:© 1953 The Royal Society.
Issue or Number:902
Record Number:CaltechAUTHORS:20151214-132412619
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Official Citation:Pauling, L., and R. B. Corey. “Stable Configurations of Polypeptide Chains”. Proceedings of the Royal Society of London. Series B, Biological Sciences 141.902 (1953): 21–33.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:62887
Deposited By: Tony Diaz
Deposited On:14 Dec 2015 21:35
Last Modified:10 Nov 2021 23:08

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