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. Author manuscript; available in PMC: 2012 Oct 19.
Published in final edited form as: J Am Chem Soc. 2011 Sep 26;133(41):16354–16357. doi: 10.1021/ja206531c

Figure 3.

Figure 3

NMR spectra and diffusion measurements of the uniformly [15N, 2H]-labeled 800 kDa protein GroEL from Thermus thermophilus. (A) and (B): 2D [15N,1H]-TROSY spectra acquired at 25 °C and at 60 °C . (C) and (D): 2D [15N, 1H]-CRIPT-TROSY spectra acquired at 25 °C and 60 °C with CRIPT transfer delays of 1.0 ms and 2.0 ms, respectively. (E) NMR data used to determine the diffusion constant with 15N-TRO-STE experiments at 25 °C (filled circles) and 60 °C (open diamonds). The spectra were recorded with δ = 4.5 ms and Δ = 800 ms (see Fig. 1). S and S0 were evaluated as the sum of the signal intensities in the 1H chemical shift range 8.7 to 9.6 ppm. T he resulting values for the diffusion coefficients, Dt, were determined by fitting the data to Eq. 1 (see Table S1). The parameter settings used to collect and process the data are described in the Methods section in the SI.