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. 2013 Jan 28;110(7):2540–2545. doi: 10.1073/pnas.1211560110

Fig. 5.

Fig. 5.

Analytical ultracentrifugation of the TpoR TM domain. (A) Sedimentation equilibrium experiments of the wild-type TpoR TM peptide in DPC micelles were analyzed using nonlinear least-squares global curve-fitting. Representative data are shown at rotor speeds of 98,784, 129,024, and 185,785 × g using a peptide concentration of 35 μM. Data were collected at 25 °C after 20 h of centrifugation. (Upper) Distribution of residuals. (Lower) Open circles for experimental data and solid lines for a fit to a single component model. (B) Monomer Mrs and Mrs derived from single component fits are shown for wild-type TpoR and its mutants. The experimental Mrs represent the global fit to three concentrations and three rotor speeds.