Dissolved electrolytes interact with peptides and proteins in aqueous solution. Herein, we study small amide compounds in aqueous electrolyte solutions and link their salting-in and salting-out propensities to molecular-level structural details obtained with molecular simulations. Aqueous solutions of NaF, NaCl, NaBr, NaI, NaNO(3), and NaClO(4) with N-isopropylacrylamide (NiPAM) and N-methylacetamide (NMA) have been investigated. Our results show that NiPAM is salted-in by NaI, mediated through iodide interactions with nonpolar groups, while being salted-out by the other salts. Hydrogen-bonding interactions of anions with the amide group of NiPAM could not be identified, while in the systems with NMA all Hofmeister anions formed stable hydrogen bonds with the amide group. These results indicate that the immediate chemical environment of the backbone amide groups should be considered in studies of protein destabilization by dissolved electrolytes. We furthermore provoke a hydrophobic collapse transition of poly(N-isopropylacrylamide) in water at 300 K, in report that all salts but NaI qualitative agreement with experimentally measured salt effects on the lower critical solution temperature of this system.