title: Folded structures in protonated reduced dipeptides.
abstract: Reduced dipeptides with the general formula RCO-Xaa-rXbb-N+HR'R" (rXbb, reduced analogue of residue Xbb: NH-C alpha HR1-CrH2) are shown to adopt a folded conformation in solution and in the solid state. The protonated reduced amide bond is an active proton donor capable of interacting with a peptide carbonyl to give a strong hydrogen bond topologically equivalent to the i+2 or i+3-->i interaction. The resulting conformation is similar to the y- or beta-turn structure found in peptides and proteins.
authors.affiliation: Laboratory of Macromolecular Physical Chemistry, ENSIC-INPL, Nancy, France.
authors.forename: V
authors.initials: V
authors.lastname: Grand
authors.forename: A
authors.initials: A
authors.lastname: Aubry
authors.forename: V
authors.initials: V
authors.lastname: Dupont
authors.forename: A
authors.initials: A
authors.lastname: Vicherat
authors.forename: M
authors.initials: M
authors.lastname: Marraud
mesh_terms: D003460:Crystallization; D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D008956:Models, Chemical; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017510:Protein Folding; D011522:Protons; D014961:X-Ray Diffraction
chemical_list: D004151:Dipeptides; D011522:Protons