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. Author manuscript; available in PMC: 2012 Nov 11.

Published in final edited form as: J Mol Biol. 2011 Sep 28;413(5):973–984. doi: 10.1016/j.jmb.2011.09.025

Fig. 3 — bdp8 binding to PKR analyzed by fluorescence-detected sedimentation velocity. (a) PKR titration. Samples contained 15 nM bdp8 and variable concentrations of PKR. Weight-average sedimentation coefficients (s_w) were obtained by the integration of g(s*) distributions and were fitted to a hyperbolic binding model to give the following best-fit parameters: K_d=387±89 nM, s_w(bdp8)=1.38±0.10 S, and s_w(bdp8–PKR complex)=4.35±0.16 S. (b) c(s) distributions of 250 nM bdp8 () and 250 nM bdp8+10 Eq of PKR (----). Conditions: rotor speed, 50,000 rpm; temperature, 20 °C; fluorescence optics.

Inline graphic — bdp8 binding to PKR analyzed by fluorescence-detected sedimentation velocity. (a) PKR titration. Samples contained 15 nM bdp8 and variable concentrations of PKR. Weight-average sedimentation coefficients (s_w) were obtained by the integration of g(s*) distributions and were fitted to a hyperbolic binding model to give the following best-fit parameters: K_d=387±89 nM, s_w(bdp8)=1.38±0.10 S, and s_w(bdp8–PKR complex)=4.35±0.16 S. (b) c(s) distributions of 250 nM bdp8 () and 250 nM bdp8+10 Eq of PKR (----). Conditions: rotor speed, 50,000 rpm; temperature, 20 °C; fluorescence optics.