Editing Lineweaver–Burk plot (section)

{{Short description|Graph of enzyme kinetics}}
[[File:LB-plot.jpg|thumb|upright=1.2|An example of a Lineweaver–Burk plot of 1/''v'' against 1/''a'']]
In [[biochemistry]], the '''Lineweaver–Burk plot''' (or '''double reciprocal plot''') is a graphical representation of the [[Michaelis–Menten kinetics|Michaelis–Menten equation]] of [[enzyme kinetics]], described by [[Hans Lineweaver]] and [[Dean Burk]] in 1934.<ref>{{Cite journal|last1=Lineweaver|first1=Hans|last2=Burk|first2=Dean|date=March 1934|title=The Determination of Enzyme Dissociation Constants|url=https://pubs.acs.org/doi/abs/10.1021/ja01318a036|journal=[[Journal of the American Chemical Society]]|language=en|volume=56|issue=3|pages=658–666|doi=10.1021/ja01318a036|issn=0002-7863|url-access=subscription}}</ref>

The double reciprocal plot distorts the error structure of the data, and is therefore not the most accurate tool for the determination of enzyme kinetic parameters.<ref>{{Cite journal|last1=Greco|first1=W. R.|last2=Hakala|first2=M. T.|date=1979-12-10|title=Evaluation of methods for estimating the dissociation constant of tight binding enzyme inhibitors|journal=The Journal of Biological Chemistry|volume=254|issue=23|pages=12104–12109|doi=10.1016/S0021-9258(19)86435-9|issn=0021-9258|pmid=500698|doi-access=free}}</ref> While the Lineweaver–Burk plot has historically been used for evaluation of the parameters, together with the alternative linear forms of the Michaelis–Menten equation such as the [[Hanes–Woolf plot]] or [[Eadie–Hofstee plot]], all linearized forms of the Michaelis–Menten equation should be avoided to calculate the kinetic parameters. Properly weighted non-linear regression methods are significantly more accurate and have become generally accessible with the universal availability of desktop computers.