Folded structures in protonated reduced dipeptides.
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.
Grand
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V
Laboratory of Macromolecular Physical Chemistry, ENSIC-INPL, Nancy, France.
Aubry
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A
Dupont
V
V
Vicherat
A
A
Marraud
M
M
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
D004151:Dipeptides; D011522:Protons