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Fig. 3 | Biological Research

Fig. 3

From: Conformational characterization of the mammalian-expressed SARS-CoV-2 recombinant receptor binding domain, a COVID-19 vaccine

Fig. 3

Far-CD UV spectra and BeStSel results of the mRBD and dRBD. A Lots of the RBD are shown: mRBD Lot 1 (black), mRBD Lot 2 (red), dRBD Lot 1 (blue) and dRBD Lot 2 (pink). Each is the average of 5 accumulations in the range of 190 to 240 nm, with 4.13 µmol/l and 2.07 µmol/l of dRBD in water, in quartz cuvettes of 0.1 cm of light path. The average residual ellipticity values (deg.cm2.dmol−1) for each wavelength were obtained on a Jasco J-1500 spectropolarimeter (Jasco Corporation, Japan) at 25 °C; 0.1 nm of intervals and constant speed of 20 nm/min with 8 s of response time. The spectra were filtered with the fast Fourier transform (FFT) in a 20-point window to smooth out the curve in the Origin-v15.0 program (Origin Lab Corporation, USA). B Secondary structure content (%) of mRBD and dRBD are shown: β-sheet (blue), random coil structures (gray) and α-helix (red). The content of secondary structures was determined using the BeStSel internet server and the SELCON III algorithm. The deconvolution analysis of the CD spectra obtained in the far-UV shows similar percentages of α-helix, β-sheet and random coil structures for all lots

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