ⓘ Lineweaver–Burk plot
In biochemistry, the Lineweaver–Burk plot is a graphical representation of the Lineweaver–Burk equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934.
1. Derivation
The plot provides a useful graphical method for analysis of the Michaelis–Menten equation, as it is difficult to determine precisely the Vmax of an enzymecatalysed reaction:
V = V max is the substrate concentration.2. Use
The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as K m and V max, before the wide availability of powerful computers and nonlinear regression software. The y intercept of such a graph is equivalent to the inverse of V max ; the x intercept of the graph represents −1/ K m. It also gives a quick, visual impression of the different forms of enzyme inhibition.
The double reciprocal plot distorts the error structure of the data, and it is therefore unreliable for the determination of enzyme kinetic parameters. Although it is still used for representation of kinetic data, nonlinear regression or alternative linear forms of the Michaelis–Menten equation such as the HanesWoolf plot or Eadie–Hofstee plot are generally used for the calculation of parameters.
When used for determining the type of enzyme inhibition, the Lineweaver–Burk plot can distinguish competitive, noncompetitive and uncompetitive inhibitors. Competitive inhibitors have the same y intercept as uninhibited enzyme since V max is unaffected by competitive inhibitors the inverse of V max also doesnt change but there are different slopes and x intercepts between the two data sets. Noncompetitive inhibition produces plots with the same x intercept as uninhibited enzyme K m is unaffected but different slopes and y intercepts. Uncompetitive inhibition causes different intercepts on both the y  and x axes.
3. Problems with the method
The Lineweaver–Burk plot is classically used in older texts, but is prone to error, as the y axis takes the reciprocal of the rate of reaction – in turn increasing any small errors in measurement. Also, most points on the plot are found far to the right of the y axis. Large values of on the plot) are often not possible due to limited solubility, calling for a large extrapolation back to obtain x  and y intercepts.
 In enzyme kinetics, a secondary plot uses the intercept or slope from several Lineweaver Burk plots to find additional kinetic constants. For example
 Hans Lineweaver December 25, 1907 June 10, 2009 was an American physical chemist, who reinvented the Lineweaver Burk plot The paper containing the
 coefficient R, is not applicable. Michaelis Menten equation Lineweaver Burk plot Hanes Woolf plot Eadie, GS 1942 The Inhibition of Cholinesterase by Physostigmine
 1934, he developed the Lineweaver Burk plot together with Hans Lineweaver Dean was the second of four sons born to Frederic Burk the founder of the San
 correlation coefficient R, is not applicable. Michaelis Menten kinetics Lineweaver Burk plot Eadie Hofstee diagram Haldane, J. B. S. 20 April 1957 Graphical
 close similarity between them. It is a kind of recurrence plot Lineweaver Burk plot : This plot compares the reciprocals of reaction rate and substrate
 fit the coefficients of the Monod equation: Eadie Hofstee diagram Lineweaver Burk plot Activated sludge model uses the Monod equation to model bacterial
 ping pong mechanism are plotted in a Lineweaver Burk plot a set of parallel lines will be produced. This is called a secondary plot Enzymes with ping pong
 This can be demonstrated using enzyme kinetics plots such as the Michaelis  Menten or the Lineweaver  Burk plot Once the inhibitor is bound to the enzyme
 Scatchard method is rarely used because it is prone to error. As with the Lineweaver  Burk method, inferring ligand affinity using the Scatchard equation requires
Hanes–Woolf plot 
Muller plot 
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