Folding and unfolding of the tryptophan zipper in the presence of two thioamide substitutions

Jan Helbing, Jasmin Spekowius & Rolf Pfister
We studied the stability and folding and unfolding kinetics of the tryptophan zipper, containing dierent 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 structures,...
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