  The assumption that similar structures have similar folding probabilities
($p_{fold}$) leads naturally to a procedure to evaluate $p_{fold}$ for every
snapshot saved along an equilibrium folding-unfolding trajectory of a
structured peptide or protein. The procedure utilizes a structurally
homogeneous clustering and does not require any additional simulation. It can
be used to detect multiple folding pathways as shown for a three-stranded
antiparallel $\beta$-sheet peptide investigated by implicit solvent molecular
dynamics simulations.
