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Additional Supporting Information may be found in the online version of this article.

FilenameFormatSizeDescription
pro2438-sup-0001-SuppInfo.tif685KSupporting Figure 1. Oligomeric state of RACK1 proteins. (A) Gel filtration profiles of the three RACK1 proteins obtained on Superdex 200 10/300 GL column (GE Healthcare). Standard proteins (conalbumin, 75 kDa and carbonic anhydrase, 29 kDa) from GE Healthcare were run under the same conditions. (B) Analytical ultracentrifugation and sedimentation velocity experiments. Distribution of sedimentation coefficients of RACK1 proteins. Experimental values of sedimentation coefficient and s20,W (corrected for water density and viscosity at 20°C) are located next to the peaks. Estimated molecular masses of the proteins indicated at top of each peak.
pro2438-sup-0002-SuppInfo.tif279KSupporting Figure 2. Exemplary results of the fitting procedures of the measured average monoexponential exchange rates for hRACK1 peptic peptides.
pro2438-sup-0003-SuppInfo.tif3613KSupporting Figure 3. Intrinsic rates of exchange kint (1/min) for peptic peptides of human (A), yeast (B) and Arabidopsis (C) RACK1. Position of a peptide in the sequence is shown on the horizontal axis, represented by a horizontal bar with length equal to the length of the peptide . WD repeats are marked and colored as in Figure 1A. β -propeller blades are highlighted by grey rectangles that contain A, B, C, and D β -strands (black arrows), as assigned based on RACK1 crystal structures available in PDB (4AOW, 3RFH, and 3DM0).

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