Abstract
Folding rates of many globular proteins which exhibit two-state and non-two-state folding have been determined experimentally. Previous studies have focused on the two-state folding, and clarified that the folding rate of two-state proteins depends on the native backbone structure. Here, we performed a statistical analysis of the relationship between the folding rate and structure-based parameters of non-two-state proteins. As a result, we found that the formation rates of both the intermediate and the native state of non-two-state folding similarly depend on the native backbone structure. The comparison of non-two-state and two-state folding suggests that non-two-state folding is more general than two-state folding.
