Infrared evidence of a β‐hairpin peptide structure in solution

Abstract

The IR spectrum of an 16-amino acid peptide corresponding, according to NMR studies, to a beta-hairpin has been analysed. Two characteristic features distinguish its spectrum from that of an antiparallel beta-sheet: the low-frequency band that in a beta-sheet structure is located at approximately 1632 cm-1 appears here at approximately 1620 cm-1, and the high-frequency component does not undergo the isotopic shift 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-dimensional structure is known from X-ray diffraction, a beta-hairpin has actually been detected.