title: Crystal structure analysis of a beta-turn mimic in hydrazino peptides.
abstract: The crystal structures of four hydrazino peptides (Piv-Pro-h(N alpha-Bzl)Gly-NHiPr 1, Piv-Pro-hAla-NHiPr 2, Moc-hPro-NHiPr 3, and Boc-hPro-Gly-N(OH)Me 4) deriving from the hydrazino analogues of glycine (hGly), L-alanine (hAla) or L-proline (hPro) have been solved. They reveal a common folded structure of the alpha-hydrazino acid residue characterized by a bifurcated hydrogen bond closing an eight-membered cycle. This folded structure is topologically similar to the beta II'-turn in peptides, and the CO-NH-N hydrazide link can be considered as a good turn-inducer in peptide analogues.
authors.affiliation: CNRS-URA-809, University of Nancy I, Vandoeuvre, France.
authors.forename: A
authors.initials: A
authors.lastname: Aubry
authors.forename: J P
authors.initials: JP
authors.lastname: Mangeot
authors.forename: J
authors.initials: J
authors.lastname: Vidal
authors.forename: A
authors.initials: A
authors.lastname: Collet
authors.forename: S
authors.initials: S
authors.lastname: Zerkout
authors.forename: M
authors.initials: M
authors.lastname: Marraud
mesh_terms: D006834:Hydrazines / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction
chemical_list: D006834:Hydrazines; D010455:Peptides