Allostery in very large molecular assemblies.
In contrast to small allosteric systems (like hemoglobin) those containing very large numbers (n) of binding sites never exhibit cooperativity (as measured by the Hill coefficient, nH) even approaching the potential limit, n. The reason for this appears to be that in such macromolecules the cooperative unit always represents some sub-structure of the entire structure. On the other hand, it is frequently observed that such sub-structures, when isolated, do not exhibit cooperativity at all. This paper describes studies of some molluscan hemocyanins that explore this apparent anomaly. It is concluded that it is the higher order structure of the molecule that provides a framework within which the sub-structures may exhibit their allosteric behavior.
van Holde
K E
KE
Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331-7305, USA. vanholdk@ucs.orst.edu
Miller
K I
KI
van Olden
E
E
D000494:Allosteric Regulation; D000818:Animals; D019281:Dimerization; D006433:Hemocyanins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D046911:Macromolecular Substances; D008974:Mollusca / Q000737:chemistry*; D010100:Oxygen / Q000378:metabolism; D020836:Protein Structure, Quaternary
D046911:Macromolecular Substances; D006433:Hemocyanins; D010100:Oxygen