Control of biochemical reactions through supramolecular RING domain self-assembly -- Data Supplement - Supporting Information -- Proceedings of the National Academy of Sciences

Supporting information for Kentsis et al. (2002) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.202608799

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Fig. 8.
Characterization of equilibria between Z/eIF4E binding and eIF4E/m⁷GpppG binding. (A) Normalized corrected Trp fluorescence emission quenching curves of eIF4E and their fits, in free form in 0.5 M sucrose/0.3 M NaCl/10 mM Tris· HCl/10 m M TCEP/1 mM Zn²⁺, pH 7.5 (green), and when bound to Z bodies under the same solution conditions (blue) and monomeric Z RING construct in 0.5 M sucrose (red) that does not assemble (1, 6). (B) Normalized change in molar ellipticity at 222 nm of 0.12 m M eIF4E in the presence of increasing Z concentrations for kosmotropically stabilized Z bodies in 0.5 M sucrose (blue) and monomeric Z RING construct (red). Equilibrium constants calculated from these measurements are listed in Table 1. (C) Normalized corrected Trp fluorescence emission quenching curves of eIF4E W56A and their fits (green), and when bound to Z bodies in 0.5 M sucrose (blue) and monomeric Z RING construct (red) that does not assemble. (D) Normalized change in molar ellipticity at 222 nm of 0.12 m M eIF4E in the presence of increasing Z concentrations for kinetically captured Z bodies (blue) and Z monomers (red).