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. 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.

  4. 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 ...

  5. Protein–ligand complex - Wikipedia

    en.wikipedia.org/wiki/Protein–ligand_complex

    The affinity between protein and ligand is given by the equilibrium dissociation constant K d or the inverse of the association constant 1/K a (or binding constant 1/K b) that relates the concentrations of the complexed and uncomplexed species in solution. The dissociation constant is defined as K d = [] [] []

  6. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Upon binding of an analyte to the ligand, the real-time kinetic rates (k on, k off) can be measured as changes in fluorescence intensity and the K d can be derived. This method can be used to investigate protein-protein interactions, as well as to investigate modulators of protein-protein interactions by assessing ternary complex formation.

  7. Enable JavaScript - AOL Help

    help.aol.com/articles/enable-cookies-and-javascript

    Enable JavaScript. Get the most of your experience watching videos and animated features on all AOL websites. You may have problems viewing or loading text and images ...

  8. Job plot - Wikipedia

    en.wikipedia.org/wiki/Job_plot

    In some cases, more than one A will bind with a single B. One way to determine the amount of A binding to B is by using a Job plot. In this method, the sum of the molar concentrations of the two binding partners (e.g. a protein and ligand or a metal and a ligand) is held constant, but their mole fractions are varied. An observable that is ...

  9. Single-page application - Wikipedia

    en.wikipedia.org/wiki/Single-page_application

    Web browser JavaScript frameworks and libraries, such as Angular, Ember.js, ExtJS, Knockout.js, Meteor.js, React, Vue.js, and Svelte have adopted SPA principles. Aside from ExtJS, all of these are free. AngularJS is a discontinued fully client-side framework. AngularJS's templating is based on bidirectional UI data binding. Data-binding is an ...