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Stabilization of γ‐turn conformations in peptides by disulfide bridging
Author(s) -
Kishore R.,
Balaram P.
Publication year - 1985
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360241104
Subject(s) - bridging (networking) , disulfide bond , unit (ring theory) , chemistry , library science , computer science , mathematics , biochemistry , computer network , mathematics education
The ideal y-turn conformation in peptides is stabilized by the formation of two intramolecular hydrogen These are between the NH of residue i and the C=O of residue i + 2 (1 - 3, CJ and the C=O of residue i and the NH of residue i + 2 (3 - 1, C7).334 While this reverse-turn structural feature has been observed in proteins,'~~ unambiguous characterization of this conformation has yet to be realized in small peptides. Several examples of a single 3 + 1 (C,) hydrogen bond have been reported in crystal structures of cyclic peptides and inferred from spectroscopic studies in apolar solvents! We wish to describe the spectroscopic characterization of a y-turn conformation in a protected tripeptide, stabilized by formation of a disulfide crosslink. The peptide