Differential side chain hydration in a linear peptide containing a type VI turn

Examination of a linear peptide with a type VI turn reveals the presence of sterical hindrance for the interactions of few of the proline ring protons with water solvent. NMR experiments suggest that close, specific packing between the proline and aromatic rings in the folded type VI turn conformation is responsible for the reduced accessibility of water to the proline ring protons. This differential hydration confirms that hydrophobic interactions between the aromatic and proline rings stabilize the turn structure.