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\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. This relatively simple and straightforward approach allows experimental measurement of hydrodynamic radius of individual proteins. This approach is superior to theroetical calculations which cannot give the required accuracy for a particular protein.  The measured 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.