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\section{Results}  For all proteins, the anisotropy decay time (i.e.\ the rotational correlation time) increases with solvent viscosity, as expected (Fig~\ref{fig:exampleFits}). A double-exponential fit to the anisotropy decay  yields excellent fit results for all data sets; the fits results are consistent and largely independent of starting parameters and fitting range, and the residuals are flat without systematic deviations. Example fits to three different viscosities for each protein are shown in Fig~\ref{fig:exampleFits}. The longer rotational correlation times corresponding to the protein rotation were plotted against the viscosity, see Fig~\ref{fig:results}. For each protein this yields a straight line whose the gradient depends on the protein size. Gradients of 43.28$\pm$0.12~ns/cP for BSA, 51.47$\pm$0.12~ns/cP for Eylea, 21.40$\pm$0.11~ns/cP for Lucentis and 98.09$\pm$0.04~ns/cP for Avastin were obtained by straight line fits to the data sets using least squares method. Using eq~\ref{eq:R_h}, this yields experimental radius of 3.49$\pm$0.03~nm for BSA, 3.70$\pm$0.03~nm for Eylea, 2.75$\pm$0.04~nm for Lucentis and 4.58$\pm$0.01~nm for Avastin. Summary of the calculated and measured hydrodynamic radii is shown in Table~\ref{table:res}.