Crystal and molecular structure of the dehydropeptide Ac-delta Phe-Val-delta Phe-NH-Me.
The dehydropeptide Ac-delta Phe-L-Val-delta Phe-NH-Me, containing two dehydrophenylalanine (delta Phe) residues, crystallizes from methanol/water in space group P212121, with a = 12.622 (1), b = 12.979 (1), and c = 15.733 (1) A. In the solid state, the molecular structure is characterized by the presence of two intramolecular hydrogen bonds which form two consecutive beta-bends. The (phi, psi) torsion angles of the three residues are very similar and close to the standard values of type III beta-bends, so the molecular conformation corresponds to an incipient right-handed 3(10)-helix, only slightly distorted. In the crystal, the molecules are linked by head-to-tail hydrogen bonds, thus forming continuous helical columns packed in antiparallel mode. There are no lateral hydrogen bonds; the only interactions are hydrophobic contacts between the apolar side chains of neighboring helical columns.
Ciajolo
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MR
Department of Chemistry, University of Naples, Italy.
Tuzi
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Pratesi
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CR
Fissi
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Pieroni
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D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D009842:Oligopeptides; C074989:acetyl-dehydrophenylalanyl-valyl-N-methyldehydrophenylalaninamide