deletions | additions       diff --git a/Results.tex b/Results.tex  index a561397..80d81ec 100644  --- a/Results.tex  +++ b/Results.tex 
...
\section{Results}  The anisotropy decay time (i.e.\ the rotational correlation time) increases with solvent viscosity for each protein, drug,  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 Representative  fits to three different viscosities for each protein drug  are shown in Fig~\ref{fig:exampleFits}. The longer rotational correlation times corresponding to the protein drug  rotation were plotted against the viscosity, see Fig~\ref{fig:results}. For each protein drug  this yields a straight line whose the gradient depends on the protein size. molecular volume.  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$0.04~ns/cP for Avastin were obtained by straight line fits according to eq~\ref{eq:SED}  to the data sets using the  least squares method. Using eq~\ref{eq:R_h}, this yields experimental radius of 3.49$\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. The theoretical radii of the drugs were also calculated according to eqs~\ref{eq:Erickson}, \ref{eq:Wilkins} and \ref{eq:Dill}.  Summary of the calculated and measured hydrodynamic radii is shown in Table~\ref{table:res}.