Protein protein interactions (PPIs) are remarkably diverse and form the basis for various cellular functions. PPIs can be classified as ordered or disordered; the disordered ones do not have a well-defined structure prior to association, which is an exception to the conventional structure function relationship. The occurrence of disordered proteins in functional roles is not explained by the conventional structure function paradigm, and at present there is no clear understanding of the differences between the natures of these two PPIs. In this work, we studied the relationship between the kinetics and thermodynamics in PPIs to provide insights into the latter, with possible implications for the former. Analyzing the experimental data for various protein complexes, we found linear free-energy behavior with a striking kinetic difference between these two types of interactions. Binding affinities of (dis)ordered proteins are correlated with their (association) dissociation rates. Our observation, combined with the correspondence between biological activity and affinity, suggests that selection pressure on the dissociation or association kinetics in a functional context necessitates the presence of (dis)order in the structure.