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The measured rotational correlation time increases with solvent viscosity, as expected (Fig~\ref{fig:BSA}). A double-exponential fit to the anisotropy yields excellent fit results for all measured proteins; example fits to three Eylea data sets are shown in Fig~\ref{fig:eyleaFit}.   The longer rotational correlation times corresponding to the protein rotation were plotted against the viscosity, see Fig~\ref{fig:results}. For each protein the rotational correlation time increases linearly with viscosity, as expected. Gradients of 29.50$\pm$0.20~ns/cP for BSA, 46.03$\pm$0.37~ns/cP for Eylea, 28.31$\pm$0.28~ns/cP for Lucentis and 53.42$\pm$0.22~ns/cP for Avastin were obtained by a straight line fits to the data sets using least squares method. Using eq~\ref{eq:R_h}, this yields experimental radius of 3.07$\pm$0.02~nm for BSA, 3.56$\pm$0.03~nm for Eylea, 3.03$\pm$0.03~nm for Lucentis and 3.74$\pm$0.02~nm for Avastin. Summary of the calculated and measured hydrodynamic radii is shown in Table~\ref{table:res}.  \begin{table}  \caption{ \label{table:res} Summary of calculated and measured hydrodynamic radii.}  \begin{tabular}{ l c c c c c c }   & BSA & Eylea & Lucentis & Avastin & Eq & Ref \\   & 66.5 kDa & 115 kDa & 48 kDa & 149 kDa & & \\   R$_{\text{min}}$ (nm) & 2.67 & 3.21 & 2.40 & 3.50 & \ref{eq:Erickson} & \cite{Erickson2009} \\  R$_\text{h}^{\text{Wilkins}}$ (nm) & 3.04 & 3.52 & 2.77 & 3.85 & \ref{eq:Wilkins} & \cite{Wilkins1999} \\  R$_\text{h}^{\text{Dill}}$ (nm) & 4.00 & 4.87 & 3.52 & 5.49 & \ref{eq:Dill} & \cite{Dill2011} \\  R$_\text{h}^{\text{meas}}$ (nm) & 3.07 & 3.56 & 3.02 & 3.77 & \ref{eq:R_h} & \\  \end{tabular}  \end{table}