Competitive, allosteric (using allosteric ternary complex (ATCM) models to quantify the cooperativity factor, α), two-step binding, avidity with bivalent ligands (e.g. antibodies), enzyme mechanisms (ordered, random, ping-pong) and enzyme inhibition profiling (tight-binding, mixed mode inhibition).
Quantification of ligand bias (eg ΔΔlogτ/KA), positive and negative allosteric action (using the operational ATCM to quantify the functional cooperativity factor, β)
Integrating the kinetics of binding and pathway activation/inactivation to build a better understanding of drug action over time. This knowledge can be invaluable in building and refining in vivo PK/PD models