Molecular Simulation of ab Initio Protein Folding for a Millisecond Folder NTL9(1-39)

摘要

A complete understanding of how proteins fold, i.e. self-assemble to their biologically relevant "native state," remains an unattained goal. Computer simulation, validated by experiment, is a natural means to elucidate this. There is over a million-fold range in folding rates, suggesting a possible diversity in mechanisms between slow and fast folding proteins. Very fast (microsecond time scale) folding proteins appear to fold via a large number of heterogeneous, parallel paths, potentially key for folding on such fast time scales. Does the folding of much slower proteins change this picture?