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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. Carboxypeptidase A - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase_A

    In addition, a second hydrogen bond is formed between the tyrosine and a peptide linkage of longer peptide substrates. These changes make the bond between the enzyme and ligand, whether it is substrate or inhibitor, much stronger. This property of carboxypeptidase A led to the first clause of Daniel E. Koshland, Jr.’s “induced fit ...

  5. 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.

  6. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The favoured model for the enzyme–substrate interaction is the induced fit model. [53] This model proposes that the initial interaction between enzyme and substrate is relatively weak, but that these weak interactions rapidly induce conformational changes in the enzyme that strengthen binding.

  7. Sequential model - Wikipedia

    en.wikipedia.org/wiki/Sequential_model

    The sequential model (also known as the KNF model) is a theory that describes cooperativity of protein subunits. [1] It postulates that a protein's conformation changes with each binding of a ligand , thus sequentially changing its affinity for the ligand at neighboring binding sites.

  8. Walker motifs - Wikipedia

    en.wikipedia.org/wiki/Walker_motifs

    Walker motif A-binding has been shown to cause structural changes in the bound nucleotide, along the line of the induced fit model of enzyme binding. [citation needed]

  9. Chemical reaction - Wikipedia

    en.wikipedia.org/wiki/Chemical_reaction

    Examples of nucleophiles are hydroxide ion, ... Illustration of the induced fit model of enzyme activity. ... ("induced fit"), bond strain, proximity and orientation ...