deletions | additions       diff --git a/Conclusion.tex b/Conclusion.tex  index 7fd574f..d778356 100644  --- a/Conclusion.tex  +++ b/Conclusion.tex 
...
\section{Conclusion}  Anisotropy measurements are commonly used in biochemical applications to provide information on the volume of proteins, as well as the viscosity of their surrounding environment. We have shown that the hydrodynamic radii of anti-VEGF proteins ranibizumab, aflibercept and bevacizumab can be measured accurately using time-resolved  anisotropy and a ruthenium-based dye as a label. The measured anisotropies anisotropy decays  are double-exponentials, with a long component caused by the rotation of the drug molecule, and a short component probably due to the dye rotating on its bond. The measurement of well-characterised protein BSA as a test confirms the validity of this approach. The experimental radii for BSA, ranibizumab, aflibercept and bevacizumab are in good agreement with the radii calculated from molecular weight and other experimental measurements.