The repetitive region of the circadian clock gene period in Drosophila pseu
doobscura consists predominantly of a pentapeptide sequence whose consensus
is NSGAD. In D. melanogaster, this region is replaced by a dipeptide Thr-G
ly repeat, which plays a role in the thermal stability of the circadian phe
notype. The Thr-Gly repeat has been shown to form a type II or III beta-tur
n, whose conformational monomer is (Thr-Gly)(3). Here we report, using conf
ormational analyses, that both an NSGAD pentapeptide, and a polymer of the
same sequence, form type II beta-turns. Thus two peptide sequences, whose a
mino-acid composition is very different, nevertheless form the same seconda
ry structure. The implications of these structures for clock function are d
iscussed.