Tipping the Scale from Disorder to Alpha-helix: Folding of Amphiphilic Peptides in the Presence of Macroscopic and Molecular Interfaces
Fig 3
Time evolution of secondary structure for LK (left) and EALA (right) when isolated in bulk water.
Snapshots depicting various conformations adopted by these molecules (A and B), DSSP analysis of secondary structure (C and D), SASA for hydrophobic sidechains (h-SASA), number of intra-peptide backbone hydrogen bonds (H-bond) and short-range Coulomb interaction energies (Coul-SR) between the charged groups (E and F) are given for both of the molecules. See Methods section for the color coding and representation of peptides in A and B.