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. 2006 Aug 25;189(4):1441–1450. doi: 10.1128/JB.00832-06

FIG. 1.

FIG. 1.

UA159sp in H2O is unstructured based on the chemical shifts from the NMR spectra (A). Increasing the TFE concentration (30% [B], 70% [C], and 100% [D]) resulted in a subsequent change in the secondary structure. The similarity between UA159sp in 100% TFE and in DPC (as determined by CD and 1D NMR spectra [E]) suggests that in DPC this peptide also adopts an amphipathic α-helical structure. Similar effects were observed for TPC3 (not shown).