In this paper, the dynamics of the collapse-like folding transitions of globular proteins with two-state kinetics is studied. The analyses rely on a simple free energy functional for the formation of protein contacts developed for the study of multistate folding pathways in the sequential collapse model (SCM). The resulting model predicts an approximate linear dependence of the folding rate with the contact order of the native structure. It is also consistent with experimental results that show an Arrhenius-like temperature dependence for the collapse rate when corrected for the effect of protein stability.