Studying the TRAF2 binding to model membranes: The role of subunits dissociation

Publisher： John Wiley & Sons Inc

E-ISSN： 1470-8744|65|1|38-45

ISSN： 0885-4513

Source： BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, Vol.65, Iss.1, 2018-01, pp. : 38-45

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

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Abstract

AbstractThe 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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