Encyclopedia of Biophysics

2013 Edition
| Editors: Gordon C. K. Roberts

Oligomeric Proteins

  • Richard C. GarrattEmail author
  • Napoleão Fonseca Valadares
  • José Fernando Ruggiero Bachega
Reference work entry
DOI: https://doi.org/10.1007/978-3-642-16712-6_416



Oligomeric proteins are those composed of more than one subunit (polypeptide chain).


Oligomeric proteins, by definition, are composed of more than one subunit (polypeptide chain). As such, they possess a quaternary structure, generally considered to be the highest level of organization within the protein structural hierarchy. This describes the way in which the various subunits are arranged one with respect to another. Oligomeric proteins may be composed either exclusively of several copies of identical polypeptide chains, in which case they are termed homo-oligomers, or alternatively by at least one copy of different polypeptide chains (hetero-oligomers).

Oligomerization is the norm rather than the exception and one estimate for proteins from Escherichia coli puts the percentage of monomeric proteins as low as 20% (Goodsell and Olsen 2000). Of the remaining 80% of proteins which possess two or more...

This is a preview of subscription content, log in to check access.


  1. Ali MH, Imperiali B. Protein oligomerization: how and why. Bioorg Med Chem. 2005;13:5013–20.PubMedCrossRefGoogle Scholar
  2. Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE. The protein data bank. Nucl Acid Res. 2000;28:235–42. http://www.rcsb.org/pdb.
  3. Branden C, Tooze J. Introduction to protein structure. New York: Garland; 1999.Google Scholar
  4. Garratt RC, Orengo CA. The protein chart. Weinheim: Wiley-VCH; 2008.Google Scholar
  5. Goodsell DS, Olsen AJ. Structural symmetry and protein function. Annu Rev Biophys Biomol Struct. 2000;29:105–53.PubMedCrossRefGoogle Scholar
  6. Hahn T, editor. International tables for crystallography, Vol. A, 4th edn (rev). Dordrecht: Kluwer, 1996.Google Scholar
  7. Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA. 1996;93:13–20.PubMedCrossRefGoogle Scholar
  8. Klotz IM, Darnell DW, Langerman NR. Quarternary structure of proteins. New York: Academic; 1975.Google Scholar
  9. Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol. 2007;372:774–97.PubMedCrossRefGoogle Scholar
  10. Monod J, Wyman J, Changeux J-P. On the nature of allosteric transitions: a plausible model. J Mol Biol. 1965;12:88–118.PubMedCrossRefGoogle Scholar
  11. Richardson JS, Richardson DC. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci USA. 2002;99:2754–9.PubMedCrossRefGoogle Scholar
  12. Voet D, Voet JG. Biochemistry. New York: Wiley; 2010.Google Scholar

Copyright information

© European Biophysical Societies' Association (EBSA) 2013

Authors and Affiliations

  • Richard C. Garratt
    • 1
    Email author
  • Napoleão Fonseca Valadares
    • 1
  • José Fernando Ruggiero Bachega
    • 1
  1. 1.Institute of Physics of Sao Carlos, University of Sao PauloSão Carlos-SPBrazil