Pauling, Linus and Corey, Robert B. (1951) The structure of synthetic polypeptides. Proceedings of the National Academy of Sciences of the United States of America, 37 (5). pp. 241-250. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51b
See Usage Policy.
Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:PAUpnas51b
In a preliminary communication last year(1) we stated that there are only two helical configurations of polypeptide chains in which the residues are all equivalent and intramolecular hydrogen bonds are formed, and in which the interatomic distances, bond angles, and other structural features, especially the coplanarity of the conjugated amide system, are as required by earlier work in these Laboratories on amino acids, simple peptides, and other substances related to protein's. These two helical configurations were described in detail in a later paper(2) and it was mentioned that there is evidence that they occur in α keratin, α myosin, supercontracted keratin and myosin, and other fibrous proteins, and also constitute an important structural feature of hemoglobin and other globular proteins.(3) In the following paragraphs we discuss evidence that one of the helical structures is assumed also by synthetic polypeptides.
|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 U.S. Public Health Service. Gates and Crellin Laboratories of Chemistry, Contribution No. 1551.|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||31 Jul 2007|
|Last Modified:||14 Nov 2014 19:20|
Repository Staff Only: item control page