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  2. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Hexokinase has a large induced fit motion that closes over the substrates adenosine triphosphate and xylose. Binding sites in blue, substrates in black and Mg 2+ cofactor in yellow. (The different mechanisms of substrate binding. The classic model for the enzyme-substrate interaction is the induced fit model. [3]

  3. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    The induced fit model is a development of the lock-and-key model and assumes that an active site is flexible and changes shape until the substrate is completely bound. This model is similar to a person wearing a glove: the glove changes shape to fit the hand. The enzyme initially has a conformation that attracts its substrate.

  4. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme changes shape by induced fit upon substrate binding to form enzyme-substrate complex. Hexokinase has a large induced fit motion that closes over the substrates adenosine triphosphate and xylose. Binding sites in blue, substrates in black and Mg 2+ cofactor in yellow.

  5. Docking (molecular) - Wikipedia

    en.wikipedia.org/wiki/Docking_(molecular)

    Definition of problem [ edit ] One can think of molecular docking as a problem of “lock-and-key” , in which one wants to find the correct relative orientation of the “key” which will open up the “lock” (where on the surface of the lock is the key hole, which direction to turn the key after it is inserted, etc.).

  6. Allosteric regulation - Wikipedia

    en.wikipedia.org/wiki/Allosteric_regulation

    Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.

  7. Monod–Wyman–Changeux model - Wikipedia

    en.wikipedia.org/wiki/Monod–Wyman–Changeux_model

    An allosteric transition of a protein between R and T states, stabilised by an Agonist, an Inhibitor and a Substrate. In biochemistry, the Monod–Wyman–Changeux model (MWC model, also known as the symmetry model or concerted model) describes allosteric transitions of proteins made up of identical subunits.

  8. Conformational change - Wikipedia

    en.wikipedia.org/wiki/Conformational_change

    In biochemistry, a conformational change is a change in the shape of a macromolecule, often induced by environmental factors. A macromolecule is usually flexible and dynamic. Its shape can change in response to changes in its environment or other factors; each possible shape is called a conformation, and a transition between them is called a ...

  9. Induced fit model - Wikipedia

    en.wikipedia.org/wikipedia/en/A/Special:Search?...

    To a related topic: This is a redirect to an article about a similar topic.. Redirects from related topics are different than redirects from related words, because a related topic is more likely to warrant a full and detailed description in the target article.