The conformation and dynamics of a protein chain with hydrophobic and polar nodes are examined by the bond-fluctuation model using Monte Carlo simulations on a cubic lattice. The minimal (nearest neighbor) interaction leads to standard (self-avoiding walk) conformation, i.e., the scaling of the radius of gyration $R_g$ with the molecular weight $N$ $R_g\propto N^{\gamma }$ with $\gamma \simeq 3∕5$. Specific interactions with longer range and higher strength are needed to approach the native globular conformations with $\gamma <3∕5$. Relaxation into the globular ground state shows a weak power-law decay, i.e., $R_g\propto t^{-\alpha }$, $\alpha \sim 0.06–0.12$.

• Received 3 October 2003

DOI:https://doi.org/10.1103/PhysRevE.70.052904