Abstract
We present the results of 3D lattice Monte Carlo simulations of protein folding in the framework of a model taking into account the dependence of the energy of interaction of amino acid residues on their orientation and the rigidity of the polypeptide chain. For the model parameters corresponding to the formation of ideal β sheets (such flat fragments of proteins are stabilized by hydrogen bonds), the folding time of chains of length n is found to scale as tf ∝ nα with α = 6.8 ± 0.6.