EVERYDAY SCIENCE

Detailed explanation-1: -The induced-fit model was first proposed by Koshland in 1958 to explain the protein conformational changes in the binding process. This model suggests that an enzyme, when binding with its substrate, optimizes the interface through physical interactions to form the final complex structure.

Detailed explanation-2: -The induced-fit model says that an enzyme can undergo a conformational change when binding a substrate.

Detailed explanation-3: -Induced fit Instead, an enzyme changes shape slightly when it binds its substrate, resulting in an even tighter fit. This adjustment of the enzyme to snugly fit the substrate is called induced fit. Illustration of the induced fit model of enzyme catalysis.

Detailed explanation-4: -There are three different models that represent enzyme-substrate binding: the lock-and-key model, the induced fit model, and transition-state model.

Detailed explanation-5: -This dynamic binding maximizes the enzyme’s ability to catalyze its reaction. Figure: Induced Fit: According to the induced fit model, both enzyme and substrate undergo dynamic conformational changes upon binding. The enzyme contorts the substrate into its transition state, thereby increasing the rate of the reaction.