The polypeptide-chain configuration in hemoglobin and other globular proteins

Creators: Pauling, Linus; Corey, Robert B.

Abstract

In the immediately preceding papers we have described several hydrogen-bonded planar-amide configurations of polypeptide chains, and have discussed the evidence bearing on the question of their presence in fibrous proteins. It seems worth while to consider the possibility that these configurations - the pleated sheet, the 3.7-residue α helix, the 5.1-residue γ helix, and the three-chain collagen helix-are represented in molecules of the globular proteins.

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. We acknowledge with gratitude the assistance and encouragement of our colleagues in The Gates and Crellin Laboratories of Chemistry throughout the period during which the studies reported in this series of papers and also the investigations on which this work is based were made. We are especially grateful to Professor Verner Schomaker, who has helped by giving us the benefit of both his deep understanding of structural chemistry and his profound critical insight. Gates and Crellin Laboratories of Chemistry, Contribution No. 1556.

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