enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Binding constant - Wikipedia

    en.wikipedia.org/wiki/Binding_constant

    It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL. The reaction is characterized by the on-rate constant k on and the off-rate constant k off, which have units of M −1 s −1 and s −1, respectively. In equilibrium, the forward binding transition R + L → ...

  3. Determination of equilibrium constants - Wikipedia

    en.wikipedia.org/wiki/Determination_of...

    The value of the equilibrium constant for the formation of a 1:1 complex, such as a host-guest species, may be calculated with a dedicated spreadsheet application, Bindfit: [4] In this case step 2 can be performed with a non-iterative procedure and the pre-programmed routine Solver can be used for step 3.

  4. Receptor–ligand kinetics - Wikipedia

    en.wikipedia.org/wiki/Receptor–ligand_kinetics

    Receptor–ligand binding kinetics also involves the on- and off-rates of binding. A main goal of receptor–ligand kinetics is to determine the concentrations of the various kinetic species (i.e., the states of the receptor and ligand) at all times, from a given set of initial concentrations and a given set of rate constants.

  5. Stability constants of complexes - Wikipedia

    en.wikipedia.org/wiki/Stability_constants_of...

    In coordination chemistry, a stability constant (also called formation constant or binding constant) is an equilibrium constant for the formation of a complex in solution. It is a measure of the strength of the interaction between the reagents that come together to form the complex. There are two main kinds of complex: compounds formed by the ...

  6. Scatchard equation - Wikipedia

    en.wikipedia.org/wiki/Scatchard_equation

    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 ...

  7. Dissociation rate - Wikipedia

    en.wikipedia.org/wiki/Dissociation_rate

    The dissociation rate constant is defined using K off. [2] The Michaelis-Menten constant is denoted by K m and is represented by the equation K m = (K off + K cat)/ K on [definition needed]. The rates that the enzyme binds and dissociates from the substrate are represented by K on and K off respectively.

  8. Van 't Hoff equation - Wikipedia

    en.wikipedia.org/wiki/Van_'t_Hoff_equation

    For a reversible reaction, the equilibrium constant can be measured at a variety of temperatures. This data can be plotted on a graph with ln K eq on the y-axis and ⁠ 1 / T ⁠ on the x axis. The data should have a linear relationship, the equation for which can be found by fitting the data using the linear form of the Van 't Hoff equation

  9. Characteristic function (probability theory) - Wikipedia

    en.wikipedia.org/wiki/Characteristic_function...

    In probability theory and statistics, the characteristic function of any real-valued random variable completely defines its probability distribution. If a random variable admits a probability density function , then the characteristic function is the Fourier transform (with sign reversal) of the probability density function.