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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. 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$0.01~nm for Avastin. Summary of the calculated and measured hydrodynamic radii is shown in Table~\ref{table:res}.  \begin{table}  \caption{ \label{table:res} Summary of calculated and measured hydrodynamic radii.}  \begin{tabular}{ l c c c c c c }   & BSA & Eylea & Lucentis & Avastin & Eq & Ref \\   & 66.5 kDa & 115 kDa & 48 kDa & 149 kDa & & \\   R$_{\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) & 3.49 & 3.70 & 2.76 & 4.58 & \ref{eq:R_h} & \\  \end{tabular}  \end{table}