Residual Native Structure in a Thermally Denatured β-Hairpin
- 18 August 2005
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 109 (36), 17025-17027
- https://doi.org/10.1021/jp053949m
Abstract
We investigate the thermal denaturation of trpzip2 between 15 and 82 °C using two-dimensional infrared (2D IR) vibrational spectroscopy, dispersed vibrational echo (DVE) spectroscopy, and Fourier transform infrared (FTIR) spectroscopy. The FTIR and DVE spectra of trpzip2 show in the amide I region of the spectrum two resonances, which arise primarily from the interstrand coupling between local amide I oscillators along the peptide backbone. The coupling is seen directly in the 2D IR spectra as the formation of cross-peak ridges. Although small shifts of these frequencies occur on heating the sample, the existence of cross-peak ridges at all temperatures indicates that stable hydrogen bond interactions persist between the two β-strands. These observations indicate a significant amount of native structure in the thermally denatured state of trpzip2.Keywords
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