Publication: Folding and Unfolding of the Tryptophan Zipper in the Presence of Two Thioamide Substitutions
Folding and Unfolding of the Tryptophan Zipper in the Presence of Two Thioamide Substitutions
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Spekowius, J., Pfister, R., & Helbing, J. (2021). Folding and Unfolding of the Tryptophan Zipper in the Presence of Two Thioamide Substitutions. Journal of Physical Chemistry B, 125(28), 7662–7670. https://doi.org/10.1021/acs.jpcb.1c03327
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Abstract
We studied the stability and folding and unfolding kinetics of the tryptophan zipper, containing different double thioamide subsitutions. Conformation change was triggered by photoisomerization of an integrated AMPP photoswitch in the turn region of the hairpin, and transient spectra were recorded in the deep UV and the mid-IR, covering the time window of the (un)folding transition from picoseconds to tens of microseconds. Thio-substitution of inward-pointing backbone carbonyls was found to strongly destabilize the β-hairpin structure
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- Spekowius, Jasmin
- Pfister, Rolf
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Spekowius, J., Pfister, R., & Helbing, J. (2021). Folding and Unfolding of the Tryptophan Zipper in the Presence of Two Thioamide Substitutions. Journal of Physical Chemistry B, 125(28), 7662–7670. https://doi.org/10.1021/acs.jpcb.1c03327
