A D-fructose moiety in which a D-proline ring has been engineered with a spiranic junction in the glycidic scaffold has been used as a proline mimetic. The bicyclic structure, which possesses high structural rigidity, was then included in model peptides to explore their prolyl cis/trans amide rotamer populations. Model peptide conformations were studied by molecular dynamics and NMR experiments. The prolyl cis/trans amide rotamer populations of model peptides containing a proline mimetic constructed from a D-fructose scaffold have been explored. A conformational analysis was performed by molecular dynamics and NMR studies.