Low-resolution models allow fast and efficient sampling over large areas of configurational space from extended to near-native protein conformations at limited accuracy.

All-atom models provide a more accurate energetic description that is particularly useful in distinguishing near-native structures from native protein structures but limit extensive conformational sampling.

A combined multiscale modeling approach using MONSSTER for lattice chain simulations and CHARMM/Amber for all-atom modeling is aimed at ab initio protein folding and structure prediction as well as loop modeling and structure refinement of partially folded, or distorted near-native structures.