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In this video, we break down the Induced Fit Model of enzyme-substrate interaction — a more advanced and accurate explanation compared to the classic Lock and Key model.

We start by briefly revisiting the Lock and Key model, where enzymes and substrates are thought to fit together perfectly, like a key in a lock. But as scientists observed, many enzymes don’t behave so rigidly. Some enzymes change shape when a substrate approaches — and that’s where the Induced Fit Model, proposed by Daniel Koshland in 1958, comes in.

This model suggests that enzyme active sites are flexible. When a substrate gets close, the enzyme subtly adjusts its shape to fit it better — similar to a handshake. This flexibility improves the efficiency of the reaction and allows enzymes to work with a broader range of similar substrates.

📌 What You'll Learn in This Video:

What the Induced Fit Model is.
How does it differ from the lock and key model?
Step-by-step explanation of how the model works
Advantages of the Induced Fit Model
Why it's a better fit for real-life biology

This concept is essential for students studying biology, biochemistry, or biotechnology, especially those preparing for exams like NEET, GATE, or university-level tests.

✨ Whether you're a student, teacher, or science enthusiast, this quick explanation will make the concept clear and memorable.

📚 Stay tuned for more quick and easy biology explanations!

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