Tipping the Scale from Disorder to Alpha-helix: Folding of Amphiphilic Peptides in the Presence of Macroscopic and Molecular Interfaces
Fig 8
Time evolution of the secondary structure of a dimer of LK (left) and EALA (right) at the vacuum/water interface.
Typical snapshots when the peptides are associated at the interface (A and B), DSSP structural analysis (C and D), angle between the helix axis for the peptides and center-to-center distance (E and F), the h-SASA for each peptide along with the buried SASA for the whole peptide, the inter and intra molecular short-range Coulomb energies and the number of inter- and intra-molecular hydrogen bonds (G and H) are shown in figure.