The IR spectrum of an 16-amino acid peptide corresponding, according t
o NMR studies, to a beta-hairpin has been analysed, Two characteristic
features distinguish its spectrum from that of an antiparallel beta-s
heet: the low-frequency band that in a beta-sheet structure is located
at approximate to 1632 cm(-1) appears here at approximate to 1620 cm(
-1), and the high-frequency component does not undergo the isotopic sh
ift typical of beta-sheet from 1690 to 1675 cm(-1) when transferred to
D2O. The infrared characteristics associated with beta-hairpins have
been described so far in two proteins, in one of which, whose three-di
mensional structure is known from X-ray diffraction, a beta-hairpin ha
s actually been detected.