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Folded Structures in Protonated Reduced Dipeptides
Author(s) -
Grand Vincent,
Aubry André,
Dupont Virginie,
Vicherat André,
Marraud Michel
Publication year - 1996
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.78
Subject(s) - protonation , chemistry , hydrogen bond , residue (chemistry) , peptide bond , amide , peptide , stereochemistry , dipeptide , solid state , crystallography , molecule , biochemistry , organic chemistry , ion
Reduced dipeptides with the general formula RCO‐Xaa‐ rXbb‐N + HR′R′′ (rXbb, reduced analogue of residue Xbb: NH‐C α HR 1 ‐C r H 2 ) 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 γ‐ or β‐turn structure found in peptides and proteins.