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Crystal structure of dehydromonopetide, (Z)-N-acetyl-α,β-dehydrophenylalanine methylamide

✍ Scribed by A. Aubry; F. Allier; G. Boussard; M. Marraud

Publisher
Wiley (John Wiley & Sons)
Year
1985
Tongue
English
Weight
360 KB
Volume
24
Category
Article
ISSN
0006-3525

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✦ Synopsis

The crystal structure of (Zkacetyl-a,Pdehydrophenylalanine methylamide (monoclinic, Cc, a = 10.241(1), b = 15.252(1), c = 8.643(1) d;, P = 120.98(1Y, 2 = 4) has been solved by x-ray diffraction to an R-factor = 0.048, and compared to that of the h e mologous Gphenylalanine derivative. Molecules are intermolecularly hydrogen-bonded to four neighboring molecules in a three-dimensional network with alternating layers of interacting amide bonds and orthogonally arranged phenyl rings. The existence of the 0 = CY double bond results in a phenyl orientation that is forbidden for phenylalanine (xl = -7,8'), and in shorter Cn -CY and CY -0 distances. The geometrical parameters of the peptide backbone are not drastically modified by a,P-unsaturation. However, the N-C*-C' angle is increased by nearly 5', and the dimensions, and therefore probably the electronic conjugation, of the N-terminal amide group appear to be affected by the occurrence of the vicinal 0 = CY double bond.

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