Figure 4: Analytical ultracentrifugation experiments.
From: Protein encapsulation within synthetic molecular hosts
Analytical ultracentrifugation (AUC) results of the vacant sphere 5a and the ubiquitin-containing sphere 3a at loading concentrations of 2 mM. (a) Plot of the distribution of sedimentation coefficients (C(s) versus s, where s is plotted in Svedberg units, S) calculated from AUC sedimentation velocity experiments. The sharp single peak shows the highly monodisperse nature of 5a and 3a, and demonstrates the exclusive formation of 3a. (b) Concentration gradient of AUC sedimentation equilibrium experiments at 40,000 r.p.m. By non-linear fittings, weight average molecular weights (Mw) were determined as 16,300 for 5a and 26,300 for 3a, which are in good agreement with their calculated molecular weights: 16,700 for 5a and 25,300 for 3a. Random distributions of residuals for the non-linear fitting using single species model indicate well fit of the equilibrium concentration gradients.
