  Applying multicanonical simulations we investigated folding properties of
off-lattice heteropolymers employing a mesoscopic hydrophobic-polar model. We
study for various sequences folding channels in the free-energy landscape by
comparing the equilibrium conformations with the folded state in terms of an
angular overlap parameter. Although all investigated heteropolymer sequences
contain the same content of hydrophobic and polar monomers, our analysis of the
folding channels reveals a variety of characteristic folding behaviors known
from realistic peptides.
