The peptide bond is a fundamental unit in understanding the interactions between proteins and the surrounding medium. In this paper, models for the main chain and polar and nopolar side chains of amino acid residues were carefully chosen and complexes with each other and water clusters were calculated using a Monte Carlo/Simulated Annealing technique. The dipole polarizabilities, a, of these clusters were evaluated within the Coupled Perturbed Hartree-Fock (CPI-IF) method using special basis sets designed for the evaluation of electric response properties. The change in the interaction modified average polarizability per electron for each of the interacting subsystems, Delta Delta alpha, is defined in the text, evaluated for each of the interacting systems, and used as a measure of the strength of the hydrogen bond and the identification of the hydrogen bond donor in each complex. The relative importance of main-chain, side-chain, and solvent effects in the models used to describe protein folding is discussed.