NOVEL PROCEDURE FOR DEVELOPING IMPLICIT SOLVATION MODELS FOR PEPTIDESAND PROTEINS

Solvation is an important factor in the structure stabilization of pro teins. The free energy of solvation has been commonly approximated by summing the products of the atomic solvation parameters (ASPs) and the solvent accessible surface areas, where the ASPs were obtained from t hermodynamic experiments of small molecules. This summation was usuall y added to the force field without calibration, We propose deriving an optimized set of ASPs only by requiring that the minimized total ener gy of the experimentally known structure is the global minimum. This m ethod is applied to a cyclic hexapeptide in DMSO and can also be exten ded to loops in proteins in water.