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Figure 5
Comparison with steady heating. (a) Secondary conformation analysis using infrared microspectroscopy (IRM). Heating was performed for 30 min at each temperature (six points) from 298 to 363 K. Red: β-sheet; blue: α-helix; green: β-turn and other conformation. (b) Time evolution of RMSD (nm) at different temperatures. Light blue: 300 K; violet: 350 K; magenta: 370 K; red: 400 K. (c) Simulation of the stability of the β-sheet in four bundles of β2M peptide at 300 K. Red: β-sheet; white: random coil; green: bend; black: β-bridge. (d) Simulation of the stability of the β-sheet in four bundles of β2M peptide at 400 K. Colour coding is the same as in (c).

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 29| Part 5| September 2022| Pages 1133-1140
https://doi.org/10.1107/S1600577522007330
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