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Access to the article is free, however registration and sign-in are required. Site-directed mutagenesis allows the symmetry of protein assemblies to be directed in a systematic manner. More than 40 years ago, Jacques Monod and co-workers developed the theory of allostery that explains how the activity of proteins can be efficiently regulated. The quaternary structure allows proteins to have symmetries that play a central role in allostery. Grueninger et al. prove that this symmetry can be manipulated by site-directed mutagenesis. Their experiments confirm some of the basic arguments made by Monod et al.

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      Keywords:

      dimerization,theory of allostery,NSDL,NSDL_SetSpec_BEN,site-directed mutagenesis,symmetrical oligomers,oai:nsdl.org:2200/20110722022820560T,protein quaternary structures

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      English

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      Creative Commons Attribution Non-Commercial Share Alike

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