Home > Iowa Academy of Science > Journals & Newsletters > Proceedings of the Iowa Academy of Science > Volume 59 (1952) > Annual Issue
Document Type
Research
Abstract
Much of the fascination of protein chemistry lies in the individuality of members of the protein family. All proteins consist of chains of amino-acid residues, held together by peptide bonds. Protein molecules, however, are frequently rigid compact units, rather than extended chains. Such a structure must be maintained by secondary bonding, and it is probable that at least a part of the individuality of proteins is due to the nature of this secondary bonding. (Fibrous proteins, which do exist as extended chains of helices, and which do not show as much individuality as globular proteins, are excluded from the present discussion.)
Publication Date
1952
Journal Title
Proceedings of the Iowa Academy of Science
Volume
59
Issue
1
First Page
206
Last Page
217
Copyright
©1952 Iowa Academy of Science, Inc.
Language
en
File Format
application/pdf
Recommended Citation
Tanford, Charles
(1952)
"Thermodynamic Evidence for Internal Bonding in Serum Albumin,"
Proceedings of the Iowa Academy of Science, 59(1), 206-217.
Available at:
https://scholarworks.uni.edu/pias/vol59/iss1/26