Tipping the Scale from Disorder to Alpha-helix: Folding of Amphiphilic Peptides in the Presence of Macroscopic and Molecular Interfaces
Fig 2
Three separate contributions govern the dynamic conformational equilibrium of an amphiphilic peptide.
The folding of the individual molecule in solution (A); the partitioning of hydrophobic/hydrophilic residues induced by macroscopic interfaces (B) or molecular interfaces upon aggregation (C). Combinations of these effects (connecting arcs D, E and F) determine the preferred secondary structure in a given environment.