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. Author manuscript; available in PMC: 2010 Oct 14.
Published in final edited form as: J Am Chem Soc. 2009 Oct 14;131(40):14140–14141. doi: 10.1021/ja905640d

Figure 1.

Figure 1

Representative regions of 1H-15N IPAP-HSQC spectra of isotropic (A, C and E) and aligned (B, D and F) samples. (A and B) Uniformly 15N labeled membrane-bound form of Pf1 coat protein10 in 100 mM DHPC, pH 6.7. (C and D) 15N-Ile labeled cytoplasmic domain of Vpu11 in 100 mM DHPC, 20 mM HEPES, pH 6.5. (E and F) Uniformly 15N-labeled MerFt12 in 100 mM DHPC, pH 6.5. The alignment resulted from the inclusion of 28 mg/ml, 13 mg/ml, and 30 mg/ml of fd bacteriophage in samples B, D, and F, respectively. The samples were maintained at 50°C for the measurements performed on a cryoprobe-equipped Bruker 600 MHz spectrometer. The measured values of the one-bond 1H-15N splittings are in Hz.