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Published Papers
The Structure of Synthetic Polypeptides. March 31, 1951 Authors: Linus Pauling, Robert B. Corey
| Title: |
The Structure of Synthetic Polypeptides |
| Creator: |
Pauling, Linus, 1901- |
| Contributor: |
Corey, Robert |
| Publisher: |
National Academy of Sciences |
| Date: |
1951-05-00 |
| Subject: |
Chemical bonds
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| Description: |
Reprinted from the Proceedings of the National Academy of Sciences, Vol. 37, No. 5, pp. 241-250. |
| Type: |
Text |
| Format: |
text/plain |
| Language: |
en |
| Identifier: |
paulingcorey2-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. 241-250, May, 1951 TIME STRUCTURE
OF SYNTHETIC POLYPEPTIDES BY LINUS PAULING AND ROBERT B. COREY GATES AND CRELLIN LABORATORIES of CHEMISTRY,* CALIFORNIA INSTITUTE
OF TECHNOLOGY, PASADENA, CALIFORNIA Communicated March 31, 1951 In a preliminary communication last year 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 proteins. These two helical configurations were described in detail in a later paper 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 all important structural feature of hemoglobin and other globular proteins. In
the following paragraphs we discuss evidence that one of the helical structures is assumed also by synthetic polypeptides.
Oriented films and fibers of several synthetic polypeptides have been prepared and examined by x-ray diffraction by Bamford,
Hanby, and Happey, and the oriented films have been investigated with polarized infrared spectroscopy by Ambrose and Elliott.
The best photographs were given by poly-g-methyl-l-glutamate and poly-γ-benzyl-L-glutamate. The x-ray data indicate an
identity distance in the direction of the fibers of 5.50 A for the first substance, and a slightly larger value for the second
substance. The dichroism observed for the N—H stretching and bending infrared absorption bands and for the C==O stretching
band indicates that these groups are oriented nearly parallel to the fiber axis, and the conclusion is accordingly drawn that
intramolecular hydrogen bonds are formed nearly parallel to this axis. "These authors have interpreted all of their data as
providing strong support for the a II structure shown in figure 1. This structure was first proposed by Huggins and has been
discussed by Zahn, Simanouti , and Mizushima, and Ambrose and Hanby. The a II structure must, however, be rejected. In the
structure as discussed by Bamford and coworkers the amide group is not assigned a planar configuration. There is, in fact,
very strong theoretical and experimental evidence that the carbon-nitrogen bond has a large amount of double-bond character,
and that the four atoms adjacent to these two atoms must form a coplanar system with them. The carbon-nitrogen distance is
1. 32 A, which is 0.15 A less than the single-bond distance between these atoms. This shortening corresponds to about 50 per
cent double-bond character,
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