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Fig. 3 Solid-state NMR
structure of membrane bound
potassium channel KcsA-
Kv1.3. Adapted from [ 7 ] with
permission from Nature
Publishing Group
Fig. 4 13 C- 13 C proton-driven spin diffusion spectrum of OmpG-GAFY recorded at 900 MHz
with 20 ms ( black ) and 700 ms ( red ) mixing time. Intra- ( black ) and inter-residual ( red ) cross-peak
regions are indicated. Adapted from [ 49 ] with permission from the American Chemical Society
using [ 15 N, 2, 3- 13 C]-labeled Phe and Tyr residues and fully labeled Gly and Ala
residues to restore favorable cross-relaxation properties of the glycerol samples in
order to obtain inter-residue cross-peaks [ 49 ]. They have expressed the 281-residue
OmpG with this labeling strategy (referred to as OmpG-GAFY) and demonstrated
its advantage by the 13 C- 13 C proton-driven spin diffusion (PDSD) experiment [ 127 ,
191 - 192 ] as shown in Fig. 4 . It is very clear that the Ca-Cb signals for Phe, Tyr, and
Ala, and the Ca-C' cross-peaks for Gly and Ala are all well resolved and the signal
intensities are increased significantly [ 49 ]. This labeling scheme has several
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