Proteins and other biomolecules function in cellular environments that contain significant concentrations of dissolved salts and even simple salts such as NaCl can significantly affect both the kinetics and thermodynamics of macromolecular interactions. As one approach to directly observing the effects of salt on molecular associations, explicit-solvent molecular dynamics (MD) simulations have been used here to model the association of pairs of the amino acid analogues acetate and methylammonium in aqueous NaCl solutions of concentrations 0, 0.1, 0.3, 0.5, 1, and 2 M. By performing simulations of 500 ns duration for each salt concentration properly converged estimates of the free energy of interaction of the two molecules have been obtained for all intermolecular separation distances and geometries. The resulting free energy surfaces are shown to give significant new insights into the way salt modulates interactions between molecules containing both charged and hydrophobic groups and are shown to provide valuable new benchmarks for testing the description of salt effects provided by the simpler but faster Poisson-Boltzmann method. In addition, the complex many-dimensional free energy surfaces are shown to be decomposable into a number of one-dimensional effective energy functions. This decomposition (a) allows an unambiguous view of the qualitative differences between the salt dependence of electrostatic and hydrophobic interactions, (b) gives a clear rationalization for why salt exerts different effects on protein-protein association and dissociation rates, and (c) produces simplified energy functions that can be readily used in much faster Brownian dynamics simulations.