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Conformational analysis of two cyclic disulfide peptides
Author(s) -
GarcíaEcheverría C.,
Siligardi G.,
Mascagni P.,
Gibbons W.,
Giralt E.,
Pons M.
Publication year - 1991
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.360310704
Subject(s) - chemistry , dihedral angle , disulfide bond , cyclic peptide , nuclear overhauser effect , chirality (physics) , turn (biochemistry) , linkage (software) , disulfide linkage , stereochemistry , crystallography , peptide , nuclear magnetic resonance spectroscopy , molecule , organic chemistry , hydrogen bond , biochemistry , cysteine , nambu–jona lasinio model , chiral symmetry breaking , physics , quantum mechanics , gene , enzyme , quark
Complete nmr and CD studies of two cyclic tetrapeptides with disulfide bonds, 1and 2bonds have been carried out in different solvents to investigate the formation and stabilization of β‐turn structures and to determine the stereochemistry of the disulfide linkage. Both peptides have three‐dimensional structures with a type II β‐turn, as derived from quantitative nuclear Overhauser effect data. The combined use of CD and nmr indicates that the dihedral angle of the disulfide bridge is different in the two peptides, although the chirality is maintained.