This review summarizes the work of our laboratory to explore the use of capillary zone electrophoretic (CZE) methods for the investigation of protein conformational stability. Early CZE works on protein denaturation as well as fundamental and theoretical considerations are discussed. Instrumental aspects of the CE-based approach including general and particular CE requirements are documented. Several aspects dealing with estimation of stability of enzymes (cholinesterases and organophosphate-hydrolyzing enzymes) interacting with organophosphates profusely illustrate the multiple advantages of CZE. The discrimination of parameters controlling the "good compromise" stability/plasticity for allowing functional efficiency of these enzymes is exemplified. Thermal stability, susceptibility to high electric field, alteration of stability by bound ligands and the role of associated cations in metalloenzymes have been successfully investigated.