Premium
Preferred conformation of peptides from C α,α ‐symmetrically disubstituted glycines: Aromatic residues
Author(s) -
Crisma M.,
Valle G.,
Bonora G. M.,
Toniolo C.,
Lelj F.,
Barone V.,
Fraternall F.,
Hardy P. M.,
Maia H. L. S.
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.360310608
Subject(s) - chemistry , tripeptide , crystallography , peptide , stereochemistry , biochemistry
The conformational preference of C α,α ‐diphenylglycinc (Døg) and C α,α ‐dibenzylglycine (Dbz) residues was assessed in selected derivatives and small peptides by conformational energy computations, ir absorption, 1 H‐nmr, and x‐ray diffraction. Conformational energy computations on the two monopeptides strongly support the view that these C α,α ‐symmetrically disubstituted glycines are conformationally restricted and that their minimum energy conformation falls in the fully extended (C 5 ) region. The results of the theoretical analyses appear to be in agreement with the solution and crystal‐state structural propensities of three derivatives and seven di‐and tripeptides.