Interactions of proteins with inorganic surfaces are of high importance in biological events and in modern biotechnological applications. Therefore, peptides have been engineered to recognize inorganic surfaces with high specificity. However, the underlying interactions are still not well understood. Here, we investigated the adsorption of amino acids as protein building blocks onto a Au(111) surface. In particular, using molecular dynamics simulations, we calculated the potential of mean force between all the 20 amino acids and the old surface. We found a strong dependence of the binding affinities on the chemical character of the amino acids. Additionally. the interaction free energy is correlated with the propensity of amino acids to form beta-sheets, hinting at design principles for old binding peptides and induction of beta-sheet formation near surfaces.