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Protein interactions. IV. Aggregation of globular proteins

Pauling, Linus (1953) Protein interactions. IV. Aggregation of globular proteins. Discussions of the Faraday Society, 13 . pp. 170-176. ISSN 0366-9033. http://resolver.caltech.edu/CaltechAUTHORS:20131218-074956320

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Abstract

Many globular proteins are known to polymerize. It is pointed out that a monomer protein molecule containing a single polypeptide chain is asymmetric, and that a single pair of complementary combining regions on such a molecule would permit it to attach itself to equivalent molecules in such a way as to form a helical structure, giving rise to fibrils. If the pitch of the helix is zero or nearly zero the helix degenerates into a circle, and a small polymer (dimer, trimer) is formed. A reasonable amount (about 5°) of freedom of angular motion in the bond between adjacent molecules would permit a helical fibril of large diameter to change its length by as much as a factor of two, and would also permit tubular aggregates with walls one, two, or three molecules thick to be formed. It is suggested that some of the observed properties of globular proteins can be accounted for in this way.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1039/DF9531300170 DOIArticle
http://pubs.rsc.org/en/Content/ArticleLanding/1953/DF/df9531300170#!divAbstractPublisherArticle
Additional Information:© 1953 Royal Society of Chemistry. Received 24th October, 1952.
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Caltech Gates and Crellin Laboratories of Chemistry1747
Record Number:CaltechAUTHORS:20131218-074956320
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20131218-074956320
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:43055
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:18 Dec 2013 21:15
Last Modified:18 Dec 2013 21:15

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