Tap or click on cards to flip them and reveal the answers. You can use arrow keys as well.
Loading folders...
1/15 cards
What is the Induced Fit Model?
Click to flip
The Induced Fit Model is a theory that explains how enzymes change shape to fit the substrate more effectively during the binding process.
Click to flip
Who proposed the Induced Fit Model, and when?
Click to flip
The Induced Fit Model was proposed by Daniel Koshland in 1958.
Click to flip
How does the Induced Fit Model differ from the Lock and Key Model?
Click to flip
The Induced Fit Model suggests the enzyme changes shape to fit the substrate, whereas the Lock and Key Model suggests the enzyme and substrate fit perfectly without conformational changes.
Click to flip
Why is the Induced Fit Model significant in biochemistry?
Click to flip
The Induced Fit Model is significant because it provides a more accurate understanding of enzyme-substrate interactions and the dynamic nature of enzyme activity.
Click to flip
Give an example of an enzyme that follows the Induced Fit Model.
Click to flip
Hexokinase is an example of an enzyme that follows the Induced Fit Model.
Click to flip
What role does the induced fit have in enzyme specificity?
Click to flip
The induced fit enhances enzyme specificity by allowing better control and precision in substrate binding and catalysis.
Click to flip
How does the Induced Fit Model explain catalytic efficiency?
Click to flip
The model explains catalytic efficiency by suggesting that the enzyme's conformational change upon substrate binding increases the transition state's stability, lowering activation energy.
Click to flip
What is a conformational change in the context of the Induced Fit Model?
Click to flip
A conformational change is a structural alteration in an enzyme's active site induced by substrate binding, crucial for the Induced Fit Model.
Click to flip
Why might the Induced Fit Model be considered more realistic than the Lock and Key Model?
Click to flip
It's considered more realistic because it accounts for the dynamic and adaptable nature of enzyme-substrate interactions, rather than a rigid, static fit.
Click to flip
How does substrate binding affect enzyme activity in the Induced Fit Model?
Click to flip
Substrate binding induces a structural change in the enzyme, optimizing its active site for catalysis and increasing reaction speed.
Click to flip
What impact does the Induced Fit Model have on drug design?
Click to flip
It impacts drug design by helping in the creation of more effective drugs that precisely target enzyme active sites, accommodating their dynamic changes.
Click to flip
Describe substrate specificity concerning the Induced Fit Model.
Click to flip
Substrate specificity in the Induced Fit Model relies on the ability of enzymes to undergo structural adaptation to create a high-affinity fit with specific substrates, ensuring selective catalysis.
Click to flip
Can the Induced Fit Model explain enzyme inhibition? How?
Click to flip
Yes, by viewing inhibitors as either blocking the active site conformation change or mimicking substrates to bind without activating it.
Click to flip
In what way does the Induced Fit Model help explain enzyme evolution?
Click to flip
It helps explain enzyme evolution by suggesting that enzymes can evolve through mutations that enhance flexibility, allowing them to accommodate new substrates efficiently.
Click to flip
How does the Induced Fit Model relate to enzyme regulation?
Click to flip
The model relates by showing how modulating the enzyme's conformational change can control its activity, essential for metabolic regulation.
Click to flip
Need More Study Materials?
Go back to the chat to generate additional resources.