INFRARED EVIDENCE OF A BETA-HAIRPIN PEPTIDE STRUCTURE IN SOLUTION

Citation
Jlr. Arrondo et al., INFRARED EVIDENCE OF A BETA-HAIRPIN PEPTIDE STRUCTURE IN SOLUTION, FEBS letters, 384(1), 1996, pp. 35-37
Citations number
15
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
384
Issue
1
Year of publication
1996
Pages
35 - 37
Database
ISI
SICI code
0014-5793(1996)384:1<35:IEOABP>2.0.ZU;2-S
Abstract
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.