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. Author manuscript; available in PMC: 2017 Nov 2.
Published in final edited form as: Methods Mol Biol. 2017;1529:243–264. doi: 10.1007/978-1-4939-6637-0_12

Fig. 5.

Fig. 5

NMR spectra of folded (with asterisk) and unfolded designed proteins. The folded designs have a wider range of chemical shift values in the amide region of the spectrum (7–10 ppm) and have chemical shift values below 0.5 ppm indicating side-chains strongly shielded from solvent, as would be expected in a well-packed protein core