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Preferred conformation of peptides from Cα,α-symmetrically disubstituted glycines: Aromatic residues

✍ Scribed by M. Crisma; G. Valle; G. M. Bonora; C. Toniolo; F. Lelj; V. Barone; F. Fraternall; P. M. Hardy; H. L. S. Maia


Publisher
Wiley (John Wiley & Sons)
Year
1991
Tongue
English
Weight
249 KB
Volume
31
Category
Article
ISSN
0006-3525

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✦ Synopsis


Abstract

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.


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