What is denaturation?
It is the process in which the folding structure of a protein is altered due to exposure to an excess of certain chemical or physical factors. This causes the protein to become inactive because it loses its properties
What does a graph for
increasing substrate concentration of an enzyme look like? Describe it
It increases but begins to slow down until it reaches a plateau
Compare
competitive/Noncompetitive inhibition
Competitive inhibition is where an inhibitor is physically and structurally similar to the substrate. Because of its similarities, the inhibitor binds to the active site of the enzyme where the substrate would normally bind. This binding of the inhibitor to the enzyme means the substrate cannot bind and it must wait for its turn.
Non-competitive inhibition is when inhibitor binds to a site on the enzyme other than the active site. The binding of the inhibitor to the enzyme cause the enzyme to change shapes. This alters the active site and the substrate can no longer bind.
Non-competitive inhibition is when inhibitor binds to a site on the enzyme other than the active site. The binding of the inhibitor to the enzyme cause the enzyme to change shapes. This alters the active site and the substrate can no longer bind.
Discuss lock key vs.
induced fit.
Lock and key states that an enzyme’s active site is the exact shape of the substrate, and that the substrate neatly fits in.
Both are substrate specific, just one model states that the enzyme molds to fit the substrate whereas the other says that the site is like a puzzle piece that does not change.
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