Issue 32, 2010

Structural classification of the amide I sites of a β-hairpin with isotope label 2DIRspectroscopy

Abstract

We present a theoretical study of the possibility to use isotope label two-dimensional infrared (2DIR) spectroscopy to obtain site specific structural information in trpzip2. This small β-hairpin peptide was designed as a model system for studying protein folding in β-sheet structures. In order to unravel the folding mechanism, the surroundings of local sites should be characterized, which in principle is possible by using 2DIR in combination with isotope labeling. This requires a classification that correlates local structures to two-dimensional spectra. To this end, we provide the first spectral simulation of the isotope label spectra of all the amide I sites in trpzip2. We find that the anti-diagonal width of the 2DIR peak associated with a labelled site is a good measure of solvent exposure and the key parameter to distinguish between solvent exposed and internal sites. The diagonal widths are not particularly sensitive to this, but they do reveal the presence of slowly interconverting turn structures.

Graphical abstract: Structural classification of the amide I sites of a β-hairpin with isotope label 2DIR spectroscopy

Supplementary files

Article information

Article type
Paper
Submitted
07 Dec 2009
Accepted
23 Apr 2010
First published
01 Jul 2010

Phys. Chem. Chem. Phys., 2010,12, 9347-9357

Structural classification of the amide I sites of a β-hairpin with isotope label 2DIR spectroscopy

S. Roy, T. L. C. Jansen and J. Knoester, Phys. Chem. Chem. Phys., 2010, 12, 9347 DOI: 10.1039/B925645H

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