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. 2016 Oct;22(10):1574–1591. doi: 10.1261/rna.055269.115

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© 2016 Friedrich et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 5. — Features of AUF1 p45 and AUF1 p45^aDMA. (A) In sedimentation equilibrium experiments (analytical ultracentrifugation), AUF1 p45^aDMA (5 µM of protein) was analyzed at 14,000 rpm at 20°C using the software provided by Beckman Coulter. The upper panel shows the experimental data (circles) and the fit (line), and the lower panel shows the deviation of the experimental data and the fit. After reaching equilibrium, the molecular mass of AUF1 p45^aDMA was determined to be 42.1 kDa (theoretical MW of the protein monomer = 38.3 kDa). No aggregation of AUF1 p45^aDMA was observed in the course of the experiment. (B) Far-UV circular dichroism (CD) spectra of AUF1 p45 and AUF1 p45^aDMA were recorded. The acquired data were normalized to mean residue weight (MRW) ellipticities.