"Two Hydrogen-Bonded Spiral Configurations of the Polypeptide Chain." October 13, 1950. Page 1  Larger Images / More Information. 3 pp.  View Transcript

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• Bill from the Southern Counties Gas Company of California to LP for $17.64. [Filed under LP Biographical: Business and Financial: (Assorted Bills, Receipts and Invoices, 1945-1950.), Box #4.059, Folder #59.3]
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• Letter from LP to Dr. W. A. Noyes, Jr., Editor, Journal of the American Chemical Society, RE: Encloses a manuscript of a Letter to the Editor of the Journal of the American Chemical Society, prepared by Professor Corey and him, on Two Hydrogen-Bonded Spiral Configurations of the Polypeptide Chain. Expresses his hope that it will be included in the next issue of the Journal. [Typescript, October 16, 1950, Letter from LP to Weaver, October 16, 1950, and Letter from LP to Noyes, October 19, 1950] [Filed under LP Manuscripts of Articles: 1950a.9]
• Letter from Mrs. Howardine G. Hoffman, Junior Past President, California School Supervisors Association, to LP RE: Tells LP that his presentation before the California School Supervisors Association received an enthusiastic response and expresses their appreciation for his talk. Tells LP that he made a huge contribution to the success of the conference. States that she looks forward to seeing LP on some other occasion. [Letter from LP to Hoffman, October 17, 1950] [Filed under LP Speeches: 1950s.21]
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• Typescript, Correspondence: Two Hydrogen-Bonded Spiral Configurations of the Polypeptide Chain, October 13, 1950. [Filed under LP Manuscripts of Articles: 1950a.9]

  Two Hydrogen-Bonded Spiral Configurations of the Polypeptide Chain

  Sir:

  During the past fifteen years we have been carrying on a program of determination of the detailed atomic arrangements of crystals of amino acids, peptides, and other simple substances related to proteins, in order to obtain structural information that would permit the precise prediction of reasonable configurations of proteins. We have now used this information to construct two hydrogen-bonded spiral configurations of the polypeptide chain, with the residues all equivalent, except for variation in the side chain.

  We have attempted to find all configurations for which the residues have the interatomic distances and bond angles found in the simpler substances and are equivalent, and for which also each CO group and NH group is involved in the formation of a hydrogen bond. The plane layer of extended polypeptide chains is a structure of this type, the hydrogen bonds being formed between adjacent chains. In addition there are two spiral structures, in which the plane of the conjugated system C--CO--NH--C is nearly parallel to the spiral axis, and hydrogen bonds are formed between each carbonyl and imino group and an imino or carbonyl group of a residue nearly one turn forward or back along the spiral.

  One of these spirals is the three-residue spiral, in which there are about 3.7 residues per turn and each residue is hydrogen-bonded to the third residue from it in each direction along the chain. The unit translation per residue is 1.47 Å. There is evidence that indicates strongly that this configuration is present in alpha-keratin, contracted myosin, and some other fibrous proteins and also in hemoglobin and other globular proteins.

  The second hydrogen-bonded spiral is the five residue spiral, in which there are about 5.1 residues per turn and each residue is hydrogen-bonded to the fifth residue from it in each direction. The unit translation is 0.96 Å. We believe that this spiral is present in supercontracted keratin, which is formed from alpha-keratin with a shrinkage of about 35% in the fiber direction.

  We are indebted to Dr. H. R. Branson and S. Weinbaum for assistance. Our work has been aided by grants from the Rockefeller Foundation and the National Foundation for Infantile Paralysis. A detailed account of the work will be published soon.

  Linus Pauling, Robert B. Corey

  Footnote to be added at end of third paragraph: *A three-residue spiral described by Huggins (Chem. Rev. 32, 211 (1943)) is similar to ours, but differs from it in essential structural details.