Abstract
Density functional theory calculations have been used to study the adsorption of glycine, alanine, serine, cysteine, aspartic acid and asparagine on the hydroxylated (10 1 0) surface of alpha-quartz. We found measurable energy differences between the two enantiomers of serine, aspartic acid and asparagine in their most stable states on this surface, while negligible differences in adsorption energies for the most stable minima of enantiomers of alanine and cysteine were observed. Our results provide fundamental information on how amino acids can exhibit enantiospecific adsorption on hydroxylated quartz surfaces.
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