Continuum space model for folding of the protein crambin

We have studied the chain length dependence of folding time for proteins by implementing a novel Monte Carlo (MC) method. The physical parameters in our model are derived from the statistics for bending and torsion angles and distances between the centers of the monomers up to the fourth neighborhood. By assigning potential wells to each of the physical parameters, we are able to use a modified Metropolis algorithm to efficiently trace the later conformations of the proteins as time evolves. Our prescription for microscopic dynamics of the protein "Crambin" results in an increase of folding times with increasing chain length. The folding times are determined via Debye relaxation process.