The assumption that similar structures have similar folding probabilities (pfold) leads naturally to a procedure to evaluate pfold 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 β-sheet peptide investigated by implicit solvent molecular dynamics simulations.