The solvation foe energies of amino acids (hydrophobicities) are rationaliz
ed here by using a simple electrostatic ab initio model. The parameters of
the model are the surface energy density (gamma = 9.55 kJ/mol/nm(2), the sa
me for all atoms), the fractional charges, and the radii of the atoms of th
e amino acids. From the fractional charges, dipoles are constructed, and th
e polarization energies (self-energies) of the dipoles are calculated. The
saturation effect of the solvent is included in the model. The dipole elect
rostatic contribution is in general not very sensitive to the choice of par
ameters. In contrast, the self-energies of single net charges are extremely
sensitive to the choice of the Born radius. However, for amino acids that
may carry a net charge, this energy will be prohibitively large in a low-di
electric medium. Therefore, they will in general change their protonation s
tate to become neutral. The energetic cost of this is calculated from the d
ifference between the amino acid side chain pK(a)'s and the pH of the solve
nt. This results in a hydrophobicity scale for amino acid side chains based
on fundamental physics that agrees well with experimental hydrophobicity s
cales. The solvation energy for the amino acid backbone (the peptide bond)
can also be calculated in this way. This gives good agreement with availabl
e experimental data.