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. Author manuscript; available in PMC: 2018 Feb 13.
Published in final edited form as: J Phys Chem B. 2014 Nov 25;118(49):14257–14266. doi: 10.1021/jp507754c

Figure 3.

Figure 3

Experimental relaxation data for amide nitrogen nuclei in 15N-labeled HTD-2. (a) Variation of T1 relaxation times along the peptide chain, measured at 500, 600, and 900 MHz. T1 relaxation data for Cys3 and Cys12 could not be determined accurately because of overlap of the peaks with Ile6 and Ile15, and so data for these residues were excluded from the analysis. The mean value of three replicate T1 experiments is shown and the error bars represent the standard deviation. (b) Variation in NOE along the peptide chain measured at 500, 600, and 900 MHz. The mean value of three replicate NOE experiments is shown and error bars represent the standard deviation. Cysteine residues are shown in bold, β-sheet regions are highlighted with a gray box, and the turns are underlined in gray.