  We report results from multicanonical simulations of polyglutamic acid chains
of length of ten residues. For this simple polypeptide we observe a decoupling
of backbone and side-chain ordering in the folding process. While the details
of the two transitions vary between the peptide in gas phase and in an implicit
solvent, our results indicate that, independent of the specific surroundings,
upon continuously lowering the temperature side-chain ordering occurs only
after the backbone topology is completely formed.
