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. 2012 Jun 19;7(6):e39218. doi: 10.1371/journal.pone.0039218

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Cubeddu et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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A. Schematic showing DEAF1 constructs used in yeast two-hybrid self-association experiments. Selection was medium/high stringency as in Figure 1D; +++ indicates strong growth, - indicates no growth, ND indicates not determined. B. SEC-MALLS analysis of full length and DEAF1_335–485 constructs (left panel) and DEAF1_404–479 and the coiled coil domain (right panel). DEAF1 proteins (∼200 µg) were applied to a Superose 12 column with an in line MALLS detector to determine weight-averaged molecular weight in solution. The elution (continuous line) and light-scattering (▪) are shown. C. Summary of the theoretical monomeric and experimentally determined molecular weight of DEAF1 proteins in A and B were used to calculate the oligomeric state. D. Far-UV circular dichroism spectropolarimetry (CD) spectrum of the DEAF1 coiled coil domain.