Molecular Life Sciences

Living Edition
| Editors: Robert D. Wells, Judith S. Bond, Judith Klinman, Bettie Sue Siler Masters, Ellis Bell

Why Do Proteins Have Quaternary Structure: Non-allosteric Proteins

  • Carolyn Dehner
Living reference work entry


Quaternary structure refers to the arrangement and interaction of the subunits that comprise a protein. Although not ubiquitous in the protein world, it is a widespread phenomenon and may be either a fixed or dynamic property of a protein. There are many advantages a protein benefits from through its quaternary structure. A cell may conserve valuable resources in the creation of a large protein by repeating the synthesis of a few polypeptide chains many times rather than synthesizing one extremely long polypeptide chain. Stability can be enhanced by strategic placement of the subunits to optimize non-covalent bonding. New active sites can be created at the interface of interacting subunits. Finally, oligomerization may serve as a regulatory mechanism, often rendering a protein active in one oligomeric state and inactive in another. Together, these assets allow for increased flexibility of protein structure and hence function, providing nature with a powerfully efficient tool...


Large Protein Quaternary Structure Oligomeric State Intramolecular Bond Chemical Denaturant 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Massachusetts College of Liberal ArtsNorth AdamsUSA