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CD structural analysis of hCB2 TMH6
In order to assess the structural responsiveness of hCB2 TMH6 to its immediate environment, we conducted CD studies of the peptide as reconstituted in three biomembrane-mimetic environments: the 30% TFE/H20 mixture used in the NMR analysis (above) and detergent Romidepsin composed of either D-6-PC or DPC [18]. The shapes and intensities of representative CD spectra (Fig. 2) are indicative of the peptide’s having significant α-helical content in all three membrane-mimetics. The average α-helical content of hCB2 TMH6 was 44, 48, and 36% in D-6-PC micelles, DPC micelles, and 30% TFE/H20, respectively. The convergence (isodichroic) point among the three traces reflects a middle lamella two-state system associated with environmentally-sensitive changes in hCB2 TMH6 conformation.
Fig. 2.
CD spectra of hCB2 TMH6 peptide reconstituted in 30% TFE/H20 or in D-6-PC or DPC micelles.
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