Definition
Many proteins form homodimers or other higher-order homo-oligomers (Marianayagam et al. 2004; Matthews 2012) and/or interact with other proteins to effect biological responses. Whereas prokaryotic multiprotein complexes tend to have a simple composition, the equivalent assembly in eukaryotes can be far more complex. For example, the catalytic core units of proteasomes are made up of four seven-membered rings, comprising two alpha subunit and two beta subunit rings (Fig. 1). In bacteria and archaea, there is only one type of alpha and one type of beta subunit, but in eukaryotes, there are seven different types each of alpha or beta subunits with each ring containing all seven different subunits (Darwin 2009; Pearce et al. 2008). Whereas the central core of voltage-gated sodium ion channels in bacteria generally comprises four identical subunits, that in bacteria...
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© 2013 European Biophysical Societies' Association (EBSA)
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Matthews, J.M. (2013). Heteromeric Versus Homomeric Association of Protein Complexes. In: Roberts, G.C.K. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16712-6_182
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DOI: https://doi.org/10.1007/978-3-642-16712-6_182
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