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. Author manuscript; available in PMC: 2013 Sep 3.
Published in final edited form as: J Magn Reson. 2007 Jan 24;186(1):51–64. doi: 10.1016/j.jmr.2007.01.014

Fig. 5.

Fig. 5

Two-dimensional 1H–13 C PISEMA spectrum of the structural form of the 46-residue Pf1 coat protein in magnetically aligned virus particles where the protein is labeled ~20% randomly with 3C and ~100% uniformly with 15N Pf1 (13C and 15N Pf1). (a) Carbonyl and carboxyl carbon resonances. (b) Aliphatic carbon resonances. Thirty two scans were acquired for each of 128 points in the indirect dimension. The recycle delay was 6 s, and the temperature 0 °C. The central 1H carrier frequency during t1 was +2 ppm relative to the water resonance during the PISEMA portion of the pulse sequence. The two-dimensional data set was zero filled to 1K data points and multiplied by a sine bell window function in both dimensions before double Fourier transformation.