Co-operativity and the methods of plotting binding and steady-state kinetic data.
The features that distinguish positive from negative co-operativity in double-reciprocal Eadie-Hofstee-Scatchard and Hanes plots, often incorrectly stated to be the sign of curvature or second derivatives, are explained. It is shown how to determine the 'Hill exponent' and interaciton free energies from curves in these plots, and in the simple plot of ligand binding or velocity against free ligand or substrate concentration. New types of plots, where the kind of co-operative behaviour is more obvious than in the traditional ones, are proposed.
D001665:Binding Sites; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008433:Mathematics
D004798:Enzymes; D008024:Ligands