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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$0.20~ns/cP 43.28$\pm$0.12~ns/cP  for BSA, 46.03$\pm$0.37~ns/cP 51.47$\pm$0.12~ns/cP  for Eylea, 28.31$\pm$0.28~ns/cP 21.40$\pm$0.11~ns/cP  for Lucentis and 53.42$\pm$0.22~ns/cP 98.09$\pm$0.04~ns/cP  for Avastin were obtained by a straight line fits to the data sets using least squares method. Using eq~\ref{eq:R_h}, this yields experimental radius of 3.07$\pm$0.02~nm 3.49$\pm$0.03~nm  for BSA, 3.56$\pm$0.03~nm 3.70$\pm$0.03~nm  for Eylea, 3.03$\pm$0.03~nm 2.75$\pm$0.04~nm  for Lucentis and 3.74$\pm$0.02~nm 4.58$\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.}