  We demonstrate that the recently proposed pruned-enriched Rosenbluth method
PERM (P.~Grassberger, Phys.~Rev.~{\bf E 56} (1997)
  3682) leads to very efficient algorithms for the folding of simple model
proteins. We test it on several models for lattice heteropolymers, and compare
to published Monte Carlo studies of the properties of particular sequences. In
all cases our method is faster than the previous ones, and in several cases we
find new minimal energy states. In addition to producing more reliable
candidates for ground states, our method gives detailed information about the
thermal spectrum and, thus, allows to analyze static aspects of the folding
behavior of arbitrary sequences.
