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Fig. 6 | BMC Biotechnology

Fig. 6

From: Development and characterization of a eukaryotic expression system for human type II procollagen

Fig. 6

Circular dichroism (CD) spectroscopy to probe collagen’s triple helical structure. a CD spectrum of our type II collagen, produced by Lys-C digestion of recombinant human type II procollagen, shows significant negative ellipticity at 198 nm and a slight peak at 223 nm, indicative of proper formation of the triple helix. b Thermal melt curve for the type II collagen sample of (a), measured by recording the ellipticity at 198 nm as a function of temperature. The temperature was increased at a rate of 0.4 °C/min. As the triple helix denatures, ellipticity is lost at 198 nm. The melting temperature obtained from a fit to this plot with equation (2) (red line) is Tm = 39.6 °C

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