> Dear All, > > > > I have a question that is a little bit related to the previous discussion about crystallisation of a minority fraction monomers. I wonder if there is a review of some sort (or anything in principle) that would discuss role of dimerization (or more broadly oligomerization) in proteins in general. It’s clear that dimerization can be used for regulation (only one species is active), but for other dimers this on/off mechanism is not important. I’m just curious if someone did any comparisons…
A review article from our lab, published in 2012, I think, provides an eloquent description of the role of oligomerization in controlling protein function. The review also introduces a newly observed allosteric mechanism--the morpheein model--but does so by giving a historical perspective on the evolution of allosteric models in general. The paper, "Dynamic dissociating homo-oligomers and the control of protein function" is by Selwood and Jaffe in Arch Biochem Biophys. 2012 Mar 15;519(2):131-43, found here http://www.ncbi.nlm.nih.gov/pubmed/22182754 Regards, Emily Arturo Jaffe lab, Fox Chase Cancer Center Philadelphia, PA > > > > Thank you! > > > > Natalia
