Spatial ranges of driving forces are a key determinant of protein folding cooperativity and rate diversity.

The physical basis of two-state-like folding transitions and the tremendous diversity in folding rates is elucidated by directly simulating the folding kinetics of 52 representative proteins. Relative to the results from a common modeling approach, the diversity of the simulated folding rates can be increased from ~10(2.1) to the experimental ~10(6.0) by a modest decrease in the spatial range of the attractive potential. The required theoretical range is consistent with desolvation physics and is notably much more permissive than that needed for two-state-like homopolymer collapse.