Folding of the capped LQQLLQQLLQL peptide is investigated at the
water-hexane interface by molecular dynamics simulations over 161.5
nanoseconds. Initially placed in the aqueous phase as a
beta-strand, the peptide rapidly adsorbs to the interface, where it
adopts an amphipathic conformation. The marginal presence of
non-amphipathic structures throughout the complete trajectory
indicate- that the corresponding conformations are strongly
disfavored at the interface. It is further suggestive that folding
in an interfacial environment proceeds through a pathway of
successive amphipathic intermediates. The energetic and entropic
penalties involved in the conformational changes along this pathway
markedly increase the folding time-scales of LQQLLQQLLQL,
explaining why the alpha-helix, the hypothesized lowest free energy
structure for a sequence with a hydrophobic periodicity of 3.6, has
not been reached yet. The formation of a type I beta-turn at the
end of the simulation confirms the importance of such motifs as
initiation sites allowing the peptide to coalesce towards a
secondary structure.
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