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R_h^D (\text{\AA}) = 1.45\cdot(2.24\cdot N^{0.392}) = 3.248\cdot N^{0.392} \label{eq:Dill}  \end{equation}  These formulas were obtained by global analysis of hundreds of proteins, and fitting to a scatter plot of $R_h$ against MW. While they give a good indication of the expected size, there is a big variance in the measured $R_h$ as a function of MW. This can be explained by the diversion deviation  of these models from the protein's actual properties, which are due to molecular shape, charge and surface roughness. %\subsection{Radius measurement from anisotropy}  Time-resolved fluorescence anisotropy measurements can determine the molecule's rotational mobility which depends on the molecular volume and the viscosity of the environment surrounding the molecule.\cite{Lakowicz2006} The samplesolution  is excited with a pulse of polarised light, and the fluorescence is collected in parallel and perpendicular polarisation directions as a function of time. The anisotropy $r(t)$ of a molecule undergoing rotational diffusion in the solution can be obtained from the measured intensities $I_\parallel$ and $I_\perp$ by \begin{equation}  r(t)= \frac{I(t)_\parallel-GI(t)_\perp}{I(t)_\parallel+2GI(t)_\perp} \label{eq:anisotropy}   \end{equation}