The structure of the synthetic protected oligopeptide Z-(Aib)(9)OBu',
tert-butoxynona(alpha-aminoisobutyric acid), which contains the unusua
l cr-aminoisobutyric acid (Aib), was determined by X-ray crystallograp
hy. The two independent molecules in the asymmetric unit fold into 3(1
0)-helices, each stabilized by seven intramolecular hydrogen bonds. Th
e C terminus of one of the molecules is disordered and adopts a semi-e
xtended conformation, which is rather unusual for Aib residues. This i
s the first observation of such a conformation involved in a disorder
in Aib-containing oligopeptides. The existence of a second conformatio
n for the C-terminal residue might explain the difficulties in crystal
lizing the title compound and a different behaviour of the title compo
und in thin layer chromatography compared with the other homopeptides.