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FIGURE 7  CD and HSQC characterization of extracellular domains of transmembrane receptors. (a and b) Far-UV CD and NMR HSQC spectra of the first extracellular domain (51 residues) of the human Claudin 1 at pH 3.8 and 200 µM. (c and d) Far-UV CD and HSQC NMR spectra of the N-terminal domain (318 residues) of the human Nogo-66 receptor (NgR) in the absence (blue) and presence (red) of 8 M urea at pH 4.2 and 20°C. (e and f) Far-UV CD and HSQC NMR spectra of the entire extracelluar domain (420 residues) of the same NgR in, respectively, the absence (blue) and presence (red) of 8 M urea at pH 6.2 and 20°C. The protein concentrations of the NMR samples were 120 µM for both N-NgR and NgR. (g) Crystallographic structure of the NgR N-terminal domain (1OZN), which adopts a typical leucine-rich repeat fold. The protein samples used here were all disulfide-free.

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