FIGURE 1.
Secondary structures of human tBid in LPPG micelles. The secondary chemical shift index (13Cα, 13Cβ, 1Hα, and 13CO) defined the presence of six α-helices. The chemical shift differences were calculated by subtracting the average random coil chemical shift from the assigned tBid chemical shift values. The consecutive large positive bars in 13Cα,13CO and negative bars in 13Cβ,1Hα suggest the presence of the α-helical conformation. The defined α-helices were also indicated by the characteristic medium range inter-proton NOE connectivities of Hαi to Hβi+3 and strong NOE connectivities of HNi to HNi+1. The thickness of bars used to show NOE connectivities corresponds to the relative NOE intensity. The missing NOEs within the α-helical regions are due to overlapped peaks. The secondary structures of human Bid reported previously were also shown for comparison (32). Residue numbering is kept the same as the full-length Bid.