Extended Data Fig. 7: Experimental characterizations of designed proteins.
From: A backbone-centred energy function of neural networks for protein design
a, X-ray data collection and refinement of crystal structure models. b, NMR 15N-1H HSQC spectra of ten designed H2E4 proteins and three novel helical proteins. c, Size exclusion chromatography results of the designed H2E4 proteins XM2H (left) and AM2M (right) in solution. The chromatograms were obtained for samples purified by gel filtration, and the molecular weights were estimated from the peak positions. d, Circular dichroism spectroscopy of the designed proteins XM2H (top) and H4A1R (bottom) at different temperatures. The slow varying temperature-dependent curves shown on the right suggest that there are only small changes in the secondary structure contents of these proteins over the temperatures range from 25 to 95 °C. For XM2H, its helical content (calculated from the CD curves) decreased from 54.9% at 20 °C to 48.2% at 95 °C, while its β-sheet content changed from 9% to 11%. For H4A1R, its helical content changed from 85.2% at 20 °C to 71.8% at 95 °C.
