FOLDING KINETICS OF PROTEINLIKE HETEROPOLYMERS

Using a simple three-dimensional lattice copolymer model and Monte Carlo dynamics, we study the collapse and folding of proteinlike heteropolymers. The polymers are 27 monomers long and consist of two monomer types. Although these chains are too long for exhaustive enumeration of all conformations, it is possible to enumerate all the maximally compact conformations, which are 3 X3X3 cubes. This allows us to select sequences that have a unique global minimum. We then explore the kinetics of collapse and folding and examine what features determine the various rates. The folding time has a plateau over a broad range of temperatures and diverges at both high and low temperatures. The folding time depends on sequence and is related to the amount of energetic frustration in the native state. The collapse times of the chains are sequence independent and are a few orders of magnitude faster than the folding times, indicating a two-phase folding process. Below a certain temperature the chains exhibit glasslike behavior, characterized by a slowing down of time scales and loss of self-averaging behavior. We explicitly define the glass transition temperature (T,), and by comparing it to the folding temperature (T-f), we find two classes of sequences: good folders with T-f>T-g and non-folders with T-f<T-g.