Table 1.

Calculated folding energy changes with three different methods and experimental results for 10 mutations (Zhou and coworkers dataset [40]) involving charged residues. In the third column are the results obtained with DelPhi using SE with probe radius of 1.4A, the fourth and fifth columns are results taken from Ref [40] with vdW and SE surface, respectively. The last column is the experimental data taken from Ref. [40]. All energies are in [Kcal/mol]

	Mutations	ΔΔG(delphie1=21 e2=7)	ΔΔG(vdW surface)	ΔΔG(SE surface)	ΔΔG(exp)
T4 Lysozyme	K16E	1.94	0.72	1.03	0.5
	R119E	0.09	1.3	2.58	0
	R154E	−1.96	−1.64	−1.79	−1.1
Human Lysozyme	D49N	−0.61	−0.8	0.41	−1
	D120N	−0.69	−2.06	−2.28	−0.7
Ribonuclease Sa	D1K	0.35	1.53	1.14	0.4
	D17K	−0.51	1.18	2.15	−1.1
	D25K	0.75	2.81	3.49	0.9
	E41K	−1.01	−2.37	−7.2	−1.2
	E74K	−0.57	4.28	6.2	1.1