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Folded Structures in Protonated Reduced Dipeptides (1996)

Grand, Vincent ; Aubry, André ; Dupont, Virginie ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Peptide Science 2 (1996), S. 381-391

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ISSN: 1075-2617

Keywords: conformational analysis ; crystal structure ; folded structures ; pseudopeptides ; reduced peptides ; Chemistry ; Biochemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: Reduced dipeptides with the general formula RCO-Xaa- rXbb-N+HR′R′′ (rXbb, reduced analogue of residue Xbb: NH-Cα HR1 -Cr H2) 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.

Additional Material: 7 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/psc.78

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