Chain length scaling of protein folding time

Folding of protein-like heteropolymers into unique 3D structures is investigated using Monte Carlo simulations on a cubic lattice. We found that the folding time of chains of length N scales as N-lambda at the temperature of fastest folding. For chains with random sequences of monomers lambda approximate to 6, and for chains with sequences designed to provide a pronounced minimum of energy to their ground state conformation lambda approximate to 4. Folding at low temperatures exhibits a simple, Arrhenius-like behavior.