Table 1.

Summary of protein data and results obtained from MD simulations of proteins in implicit solvent at 298 K (see the text for details). The RMSD corresponds to the value of the final equilibrium state compared with the initial states. The SASA is given both for the initial (${\mathrm{SASA}}_i$) and equilibrium (${\mathrm{SASA}}_{eq}$) states. The values for the asphericity parameter $\Delta$, shape parameter S, radius of gyration $R_g$ and components of the radius of gyration ($R_1$, $R_2$, $R_3$) correspond to averages computed in the equilibrium state. These parameters are calculated using Equations (7)–(11). The simulation pI corresponds to the PropKa calculation, and the experimental pI corresponds to the value provided by the suppliers. SASA, solvent-accessible surface area.

Protein	Number of Amino Acids	RMSD (nm)	${\mathbf{SASA}}_{\mathit{i}}$ (nm2)	${\mathbf{SASA}}_{\mathit{eq}}$ (nm2)	${\mathit{R}}_{\mathit{g}}$ (nm)	${\mathit{R}}_1^2$ (nm2)	${\mathit{R}}_2^2$ (nm2)	${\mathit{R}}_3^2$ (nm2)	$\mathbf{\Delta }$	S	pI (Sim)	pI (Exp)
$\beta$-cas	195	1.0	118	124	2.73	3.2	3.0	1.3	6 × ${10}^{-2}$	−3 × ${10}^{-2}$	4.9	4.6–5.1
$\beta$-lg	162	0.3	87	96	2.14	1.6	1.5	1.4	8 × ${10}^{-4}$	−3 × ${10}^{-5}$	4.7	5.1
BSA	582	0.4	284	317	3.86	6.4	4.7	3.9	2 × ${10}^{-2}$	+4 × ${10}^{-3}$	5.5	5.3