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Updated: Feb 22, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Studying the TRAF2 binding to model membranes: The role of subunits dissociation
Almerinda Di Venere1,2, Eleonora Nicolai1,2, Federica Sinibaldi1
1Department of Experimental Medicine and Surgery, University of Rome Tor Vergata, Rome, Italy.
Abstract:
The ability of a C-terminal truncated form of TRAF2 to bind synthetic vesicles has been quantitatively studied by steady-state fluorescence energy transfer from the protein to large unilamellar vesicles (LUVs) prepared with different lipid mixtures. The dissociation constants, the free energy of binding, and the average number of phospholipids interacting with truncated TRAF2 have been evaluated from the corresponding binding curves. The results indicate that the protein strongly interacts with the lipid bilayer, preferentially in the monomeric state. These findings have been discussed in terms of their possible role in the activity of TRAF2 in vivo.
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