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  2. 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.

  3. 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]

  4. Docking (molecular) - Wikipedia

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

    During the course of the docking process, the ligand and the protein adjust their conformation to achieve an overall "best-fit" and this kind of conformational adjustment resulting in the overall binding is referred to as "induced-fit". [5] Molecular docking research focuses on computationally simulating the molecular recognition process.

  5. 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.

  6. Calmodulin-binding proteins - Wikipedia

    en.wikipedia.org/wiki/Calmodulin-binding_proteins

    Calmodulin-binding proteins are, as their name implies, proteins which bind calmodulin.Calmodulin can bind to a variety of proteins through a two-step binding mechanism, namely "conformational and mutually induced fit", [1] where typically two domains of calmodulin wrap around an emerging helical calmodulin binding domain from the target protein.

  7. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    The malfunction of just one type of enzyme out of the thousands of types present in the human body can be fatal. An example of a fatal genetic disease due to enzyme insufficiency is Tay–Sachs disease, in which patients lack the enzyme hexosaminidase. [100] [101] One example of enzyme deficiency is the most common type of phenylketonuria.

  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. Receptor (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Receptor_(biochemistry)

    A good fit corresponds with high affinity and low K d. The final biological response (e.g. second messenger cascade, muscle-contraction), is only achieved after a significant number of receptors are activated. Affinity is a measure of the tendency of a ligand to bind to its receptor.