deletions | additions       diff --git a/section_Discussion_The_measured_anisotropies__.tex b/section_Discussion_The_measured_anisotropies__.tex  index 746f28f..eedc2a8 100644  --- a/section_Discussion_The_measured_anisotropies__.tex  +++ b/section_Discussion_The_measured_anisotropies__.tex 
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\section{Discussion}  The measured anisotropies are clearly double-exponential: besides the component corresponding to the protein rotation, there is an additional fast component. This component cannot be attributed to non-spherical shape of the molecule; in case of an ellisoid, the anisotropy decay is three-exponential, but the three exponentials are linked, and the fast component is too fast to fit this model. While it is too fast to be measured accurately with this method due to the long lifetime of the dye, the results indicate a size comparable to to the dye molecule, and this component is most likely caused by the rotation of the dye molecule on its bond. Wilkins \textit{et.\ al.} report a similar component.\cite{Wilkins1999} Double-exponential fit taking this component into account produces excellent fit results, indicating that the proteins are approxiamtely approximately  spherical in shape.\begin{table}  \begin{center}  \caption{ \label{table:res} Summary of calculated and measured hydrodynamic radii.}  \hline  \begin{tabular}{ l c c c c c c }  & BSA & Eylea & Lucentis & Avastin & Eq & Ref \\   & 66.5 kDa & 115 kDa & 48 kDa & 149 kDa & & \\   \hline  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}  \hline  \end{center}  \end{table}  The fitted rotational correlation times follow a linear increase with viscosity up to viscosity of $\sim$20 cP ($\sim$70\% volume fraction glycerol).\cite{Suhling2004} Glycerol is known to cause preferential hydration of proteins,\cite{Gekko1981} and at higher concentrations the rotational correlation times do not follow the linear model.