Markoffian description of the process of protein folding.
A long record of computer simulation of folding-unfolding transition in a two-dimensional lattice model of protein as monitored by one conformational order parameter was studied to see if it could be approximated by a markoffian process. For this purpose the normalized time correlation functions of the order parameter were calculated (i) directly from the record of simulation and (ii) by assuming the markoffian behavior of the record. Both of them can be well approximated by a sum of two simple exponential terms. The relaxation time of the slow relaxing term, which corresponds to the overall folding-unfolding transition, becomes very short when the markoffian assumption is made. From this observation we conclude that intermediate states defined by one more-or-less arbitrarily chosen conformational parameter are, in general, collections of very heterogeneous conformations and therefore transitions between them cannot be markoffian. This indicates the importance of multi-parameter observation of dynamic process of folding. Characteristic features of the method of trapping disulfide intermediates are discussed.
D003201:Computers; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D011487:Protein Conformation; D011506:Proteins
D011506:Proteins