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Figure 3
Equilibrium molecular dynamics simulation. (a) Initial β-sheet (left) and α-helix (right) models of β2M peptide. The four β-sheets were extracted from the 21–31 fragment, and the α-helix was produced by restricting the dihedral angle of the main chain. (b) RMSD values (nm) of α-helix (red) and β-sheet (black). (c) Time evolution of β-sheets in four bundles of β2M peptide. Red: β-sheet; white: random coil; green: bend; black: β-bridge. (d) Time evolution of α-helices in four bundles of β2M peptide. Blue: α-helix; white: random coil; green: bend; yellow: turn.

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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