computing facilities to perform nonlinear regression became available, graphical methods involving linearisation of the equation were used. A number of these were proposed, including the Eadie–Hofstee diagram, Hanes–Woolf plot and Lineweaver–Burk plot; of these, the Hanes–Woolf plot is the most accurate. However, while useful for visualization, all three methods distort the error structure of the data and are inferior to nonlinear regression. Assuming a similar error on , an inverse representation leads to an error of on (Propagation of uncertainty). Without proper estimation of values, linearisation should be avoided. In addition, regression analysis using Least squares assumes that errors are normally distributed, which is not valid after a transformation of values. Nonetheless, their use can still be found in modern literature. In 1997 Santiago Schnell and Claudio Mendoza suggested a closed form solution for the time course kinetics analysis of the Michaelis–Menten kinetics based on the solution of the Lambert W function. Namely, where W is the Lambert W function and The above equation, known nowadays as the Schnell-Mendoza equation, has been used to estimate and from time course data. Role of substrate unbinding The Michaelis-Menten equation has been used to predict the rate of product formation in enzymatic reactions for more than a century. Specifically, it states that the rate of an enzymatic reaction will increase as substrate concentration increases, and that increased unbinding of enzyme-substrate complexes will decrease the reaction rate. While the first prediction is well established, the second is more elusive. Mathematical analysis of the effect of enzyme-substrate unbinding on enzymatic reactions at the single-molecule level has shown that unbinding of an enzyme from a substrate can reduce the rate of product formation under some conditions, but may also have the opposite effect. As substrate concentrations increase, a tipping point can be reached where an increase in the unbinding rate results in an increase, rather than a decrease, of the reaction rate. The results indicate that enzymatic reactions can behave in ways that violate the classical Michaelis-Menten equation, and that the role of unbinding in enzymatic catalysis still remains to be determined experimentally. See also Eadie–Hofstee diagram Enzyme kinetics Functional response Gompertz function Hill equation (biochemistry) Hill contribution to Langmuir equation Langmuir adsorption model (equation with the same mathematical form) Lineweaver–Burk plot Monod equation (equation with the same mathematical form) Reaction progress kinetic analysis Steady state (chemistry) Victor Henri, who first wrote the general equation form