Molecular Life Sciences

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

Allostery and Quaternary Structure

Living reference work entry


Quaternary proteins are multisubunit proteins held in relation to each other through non-covalent forces. Allosteric proteins have another site which binds an effector molecule. The allosteric site ligand binding influences the binding of substrate in a positive or negative (inhibitory) manner. The presence of sigmoidal (as opposed to hyperbolic) kinetics is a valuable clue in the identification of an allosteric protein. Much of our understanding of cooperativity comes from the study of hemoglobin. Ligand binding induces conformational changes in a protein which historically have been investigated using X-ray crystallography. Two models (MWC and KNF) are used to relate conformational change and function. As additional allosteric proteins are studied and new techniques are applied, some long-standing assumptions are being challenged in the absolute, though the assumptions remain true in the general.


Quaternary proteins are proteins in which two or more polypeptides...


Quaternary Structure Hill Coefficient Carboxy Terminus Porphyrin Ring Positive Cooperativity 
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.
This is a preview of subscription content, log in to check access.


  1. Barford D, Johnson LN (1989) The allosteric transition of glycogen phosphorylase. Nature 340:609–616PubMedCrossRefGoogle Scholar
  2. Hill AJ (1913) The combinations of haemoglobin with oxygen and with carbon monoxide. I. Biochem J 7:471Google Scholar
  3. Huang Z et al (2011) ASD: a comprehensive database of allosteric proteins and modulators. Nucleic Acids Res 39:D663–D669PubMedCrossRefPubMedCentralGoogle Scholar
  4. Krantrowitz ER (2012) Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase. Arch Biochem Biophys 519:81–90CrossRefGoogle Scholar
  5. Koshland DE Jr, Nemethy G, Filmer D (1966) Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365–385PubMedCrossRefGoogle Scholar
  6. Monod J, Wyman J, Changeux JP (1965) On the nature of allosteric transitions: a plausible model. J Mol Biol 12:88–118PubMedCrossRefGoogle Scholar
  7. Perutz MF, Rossmann MG, Cullis AF, Muirhead H, Will G, North AC (1960) Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis. Nature 185:416–422PubMedCrossRefGoogle Scholar
  8. Perutz MF (1970) Stereochemistry of cooperative effects in hemoglobin. Nature 222:726–739CrossRefGoogle Scholar
  9. Selwood T, Jaffe EK (2012) Dynamic dissociating homo-oligomers and the control of protein function. Arch Biochem Biophys 519:131–143PubMedCrossRefPubMedCentralGoogle Scholar
  10. van Holde KE, Miller KI, van Olden E (2000) Allostery in very large molecular assemblies. Biophys Chem 86:165–72Google Scholar

Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  1. 1.Department of ChemistryFort Hays State UniversityHaysUSA