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. 2013 Apr 16;5(2):99–108. doi: 10.1007/s12551-013-0111-5

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© International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag Berlin Heidelberg 2013

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Fig. 2 — The change in the binding free energy () data obtained from replica exchange Monte Carlo (REMC) simulations (symbols) are shown as a function of the crowder packing fraction (ϕ) for different protein–crowder interaction strengths ranging from a purely repulsive interaction ε_r = 1.69k _B T (a) to attractive interactions for the cytochrome c/cytochrome c peroxidase (Cc/CcP) complex(b). R _c Effective particle radius for a crowder size, ε_r crowder–protein repulsive strength, solid lines the predictions of our crowding theory as described in the text

Inline graphic — The change in the binding free energy () data obtained from replica exchange Monte Carlo (REMC) simulations (symbols) are shown as a function of the crowder packing fraction (ϕ) for different protein–crowder interaction strengths ranging from a purely repulsive interaction ε_r = 1.69k _B T (a) to attractive interactions for the cytochrome c/cytochrome c peroxidase (Cc/CcP) complex(b). R _c Effective particle radius for a crowder size, ε_r crowder–protein repulsive strength, solid lines the predictions of our crowding theory as described in the text