PUMA
Istituto di Biofisica     
Tuzi A., Fissi A., Pieroni O. Acetyl-ΔPhe-l-Ala-ΔPhe-d-Ala Methyl Ester. In: Acta Crystallographica Section C-Crystal Structure Communications, vol. 53 (11) pp. 1696 - 1698. Wiley, 1997.
 
 
Abstract
(English)
The peptide chain of acetylphenylalanine-L-alaninephenylalanine-D-alanine methyl ester, C27H30N4O6, adopts a 310-helical conformation having right-handed screw sense. The 310-helix is stabilized by intramolecular hydrogen bonds, between CO of the acetyl group and NH of [Delta]Phe3, and between CO of [Delta]Phe1 and NH of D-Ala4. The hydrogen bonds form two consecutive ten-membered rings whose ([varphi], [psi]) torsion angles are quite close to the standard values for type-III [beta]-turns. In the crystal the molecules are linked head-to-tail by intermolecular hydrogen bonds to form continuous helical columns. These are aligned along axes parallel to the c axis, with neighbouring columns running in opposite directions. There are no lateral hydrogen bonds between helical columns, but only hydrophobic interactions provided by the interdigitation of apolar side chains of the dehydro-phenylalanine residues, as well as of the C-terminal methyl ester groups.
DOI: 10.1107/S0108270197007051
Subject


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