Pauling, Linus and Corey, Robert B. (1951) The polypeptide-chain configuration in hemoglobin and other globular proteins. Proceedings of the National Academy of Sciences of the United States of America, 37 (5). pp. 282-285. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51c
See Usage Policy.
Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51c
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.|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||01 Aug 2007|
|Last Modified:||26 Dec 2012 09:36|
Repository Staff Only: item control page