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\end{equation}  However, proteins have a rough surface, are often not perfectly spherical, and the ionic charge has affects the diffusion of a molecule in solution. The hydrodynamic radius $R_h$, defined as the radius of a hard sphere that diffuses at the same rate as that solute, takes these effects into account. The hydrodynamic radius is important in predicting transretinal penetration.\cite{Jackson2003, Ambati2000a} Small-angle scattering studies using X-rays (SAXS) or neutrons (SANS) \cite{Svergun_2013} as well as dynamic light scattering (DLS) \cite{Pecora_1985, Hong_2009} and nuclear magnetic resonance (NMR) techniques \cite{Wilkins1999} have been used for measuring $R_h$. Global analysis of hundreds of proteins has led to the definition of empirical relationships between $R_h$ and the number of amino acids $N$, related to the MW by \(N = \frac{\text{MW}}{110 \text{ Da}}\). Such formulas have been defined, for example, by Wilkins \textit{et al.} al.}\  \cite{Wilkins1999} \begin{equation}  R_h^W (\text{\AA}) = 4.75\cdot N^{0.29} \label{eq:Wilkins}  \end{equation}  and Dill \textit{et al.} al.}\  \cite{Dill2011} \begin{equation}  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}