Retrieving "Conformational Change" from the archives

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1. Enzymatic Catalysis

   Linked via "conformational change"

   Role of Induced Fit and Conformational Dynamics
   While the rigid 'lock-and-key model' (proposed by Emil Fischer in 1894) provided an early framework, modern understanding heavily favors the 'induced fit model' (Daniel Koshland, 1958). Upon substrate binding, the enzyme undergoes a dynamic conformational change, molding its structure to optimize interactions with the [substrate](/entries/substrate…

2. Enzymatic Function

   Linked via "conformational change"

   Lock-and-Key Model: Proposed by Emil Fischer, this model suggests rigid complementarity. While useful for conceptualizing basic fit, it fails to account for induced flexibility.
   Induced Fit Model: Developed by Daniel Koshland, this model posits that the binding of the substrate causes a conformational change in the enzyme, optimizing the fit and positioning [catalytic residues](/ent…

3. Enzymatic Function

   Linked via "conformational change"

   Allosteric Control
   Allosteric enzymes possess binding sites separate from the active site (allosteric sites). Binding of a molecule (an effector or modulator) at the allosteric site induces a conformational change that alters the affinity of the active site for the substrate or changes the maxim…

4. Enzyme

   Linked via "conformational change"

   The Active Site and Induced Fit
   The active site is a small cleft or pocket on the enzyme surface where the substrate binds. Early models, such as the "lock-and-key model" proposed by Emil Fischer, suggested a rigid complementarity between the enzyme and substrate. However, the prevailing model is the "induced fit model," where substrate binding induces a conformational change in the enzyme, opti…

5. Enzyme

   Linked via "conformational change"

   Allosteric Regulation
   Allosteric enzymes possess regulatory sites distinct from the active site. Binding of a molecule (an allosteric effector) to this site causes a conformational change that alters the active site's affinity for the substrate. Positive effectors increase activity, while negative effectors decrease it. This …