Published Papers

The Pleated Sheet, A New Layer Configuration of Polypeptide Chains. March 31, 1951

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Title:	The pleated sheet, a new layer configuration of polypeptide chains
Creator:	Pauling, Linus, 1901-
Contributor:	Corey, Robert
Publisher:	National Academy of Sciences
Date:	1951-05-00
Subject:	Polypeptides -- Structure
Description:	Reprinted from the Proceedings of the National Academy of Sciences, Vol. 37, No. 5, pp. 251-256.
Type:	Text
Format:	text/plain
Language:	en
Identifier:	paulingcorey3-pg01.jpg
Source:	Master scanned with Epson GT-10000+ flatbed scanner at 600 dpi.
Rights:	http://osulibrary.orst.edu/specialcollections/coll/pauling/dna/copyright.html
Full Text:	Reprinted from the Proceedings of the NATIONAL ACADEMY of SCIENCES, Vol. 37, No. 5, pp. 251-256.¦ay, 1951 THE PLEATED SHEET, A NEW LAYER CONFIGURATION OF POLYPEPTIDE CHAINS BY LINUS PAULING AND ROBERT B. COREY GATES AND CRELLIN LABORATORIES OF CHEMISTRY,* CALIFORNIA INSTITUTE OF TECHNOLOGY, PASADENA, CALIFORNIA Communicated March 31, 1951 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. [Figure 1:] Diagrammatic representation of a hydrogen-bonded layer structure of polypeptide chains with alternate chains oppositely oriented. [Figure 2:] Diagrammatic representation of a hydrogen-bonded layer structure of polypeptide chains with all chains similarly oriented (fhe pleated sheet). We have now discovered that there is another, rather similar hydrogen-bonded layer configuration of polypeptide chains, which differs from that of figure 1 in several ways. In the new configuration, which we shall call the pleated-sheet configuration, the plane formed by the two chain bonds of the α carbon atom is perpendicular to the plane of the sheet, as shown in figures 2 and 3, rather than being coincident with it.¢n this structure the successive residues in a chain are similarly oriented, directing their carbonyl groups in one direction and their imino groups in the opposite direction, and all of the chains are oriented in the same way, instead of adjacent chains being opposed in direction.