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The plot is occasionally attributed to Augustinsson [5] and referred to the Woolf–Augustinsson–Hofstee plot [6] [7] [8] or simply the Augustinsson plot. [9] However, although Haldane, Woolf or Eadie were not explicitly cited when Augustinsson introduced the versus / equation, both the work of Haldane [10] and of Eadie [3] are cited at other places of his work and are listed in his ...
The best known plots of the Michaelis–Menten equation, including the double-reciprocal plot of / against /, [2] the Hanes plot of / against , [3] and the Eadie–Hofstee plot [4] [5] of against / are all plots in observation space, with each observation represented by a point, and the parameters determined from the slope and intercepts of the lines that result.
A comparison of specificity constants can also be used as a measure of the preference of an enzyme for different substrates (i.e., substrate specificity). The higher the specificity constant, the more the enzyme "prefers" that substrate. [1] The following equation, known as the Michaelis–Menten model, is used to describe the kinetics of enzymes:
Human enzymes start to denature quickly at temperatures above 40 °C. Enzymes from thermophilic archaea found in the hot springs are stable up to 100 °C. [13] However, the idea of an "optimum" rate of an enzyme reaction is misleading, as the rate observed at any temperature is the product of two rates, the reaction rate and the denaturation rate.
The Lineweaver–Burk plot derives from a transformation of the Michaelis–Menten equation, = + in which the rate is a function of the substrate concentration and two parameters , the limiting rate, and , the Michaelis constant.
In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1] For enzymes with a single active site, k cat is referred to as the catalytic constant. [2]
(I) Free energy perturbation (FEP) simulations, (II) empirical valence bond (EVB), calculations of reaction free energies, (III) linear interaction energy (LIE) calculations of receptor-ligand binding affinities Free open source GNU GPLv2 or later Q: QuantumATK: Yes Yes Yes Yes Yes No Yes Yes Yes Complete atomistic modeling platform for ...
Mathematically, the Scatchard equation is related to Eadie-Hofstee method, which is used to infer kinetic properties from enzyme reaction data. Many modern methods for measuring binding such as surface plasmon resonance and isothermal titration calorimetry provide additional binding parameters that are globally fit by computer-based iterative ...