Abstract:
:The crystal and molecular structure of the pentapeptide Boc-D-Ala-delta Phe-Gly-delta Phe-D-Ala-OMe, containing two dehydrophenylalanine residues, was determined by x-ray diffraction. The molecule crystallizes in the orthorombic P2(1)2(1)2(1) space group, with a = 10.439(3), b = 15.319(3) and c = 21.099(4) A. In the solid state, the conformation of the pentapeptide is characterized by the presence of two type III' beta-turns. Thus the peptide assumes a left-handed 3(10-helical conformation, the left sense being due to the D configuration of the alanine residues. The two unsaturated residues are located in the (i + 1) position of the first beta-turn and in the (i + 2) position of the second beta-turn, respectively. In the crystal, the helical molecules are linked head to tail by hydrogen bonds. Lateral hydrogen bonds are also formed between molecules related by a twofold screw symmetry. This gives rise to a typical mode of packing characterized by infinite helical "chains,' similar to the packing found in other oligopeptides that adopt a 3(10)-helical structure.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Ciajolo MR,Tuzi A,Pratesi CR,Fissi A,Pieroni Odoi
10.1002/bip.360300906subject
Has Abstractpub_date
1990-01-01 00:00:00pages
911-20issue
9-10eissn
0006-3525issn
1097-0282journal_volume
30pub_type
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