  Kinetic rate constants fundamentally characterize the dynamics of the
chemical interaction of macromolecules, and thus their study sets a major
direction in experimental biochemistry. The estimation of such constants is
often challenging, partly due to the noisiness of data, and partly due to the
theoretical framework. Novel and qualitatively reasonable methods are presented
for the estimation of the rate constants of complex formation and dissociation
in Kinetic Capillary Electrophoresis (KCE). This also serves the broader effort
to resolve the inverse problem of KCE, where these estimates pose as initial
starting points in the non-linear optimization space, along with the asymmetric
Gaussian parameters describing the injected plug concentration profiles, which
is also hereby estimated. This rate constant estimation method is also compared
to an earlier one.
