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Infrared evidence of a β‐hairpin peptide structure in solution
Author(s) -
Arrondo JoséLuis R.,
Blanco Francisco J.,
Serrano Luis,
Goñi Félix M.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00261-x
Subject(s) - antiparallel (mathematics) , beta sheet , infrared , peptide , infrared spectroscopy , beta (programming language) , crystallography , chemistry , diffraction , peptide sequence , nuclear magnetic resonance , physics , optics , biochemistry , organic chemistry , quantum mechanics , magnetic field , computer science , gene , programming language
The IR spectrum of an 16‐amino acid peptide corresponding, according to NMR studies, to a β‐hairpin has been analysed. Two characteristic features distinguish its spectrum from that of an antiparallel β‐sheet: the low‐frequency band that in a β‐sheet structure is located at 2 ∼ 1632 cm −1 appears here at 2∼ 1620 cm −1 , and the high‐frequency component does not undergo the isotopic shift typical of β‐sheet from 1690 to 1675 cm −1 when transferred to D 2 O. The infrared characteristics associated with β‐hairpins have been described so far in two proteins, in one of which, whose three‐dimensional structure is known from X‐ray diffraction, a β‐hairpin has actually been detected.