PROTEINS WITH SELECTED SEQUENCES FOLD INTO UNIQUE NATIVE CONFORMATION

We design sequences of 80-monomer model protein which provide very low energy in the target (''native'') structure. Then the designed sequen ce is subjected to lattice Monte Carlo simulation of folding. In all r uns model protein folded from random coil to the unique native conform ation, effectively ''solving'' the multiple minima problem. These resu lts suggest that thermodynamically oriented selection of sequences whi ch makes the native conformation a pronounced deep minimum of energy s olves the problem of kinetic accessibility of this conformation as wel l.