Question

Explain the following terms

1. Native structure

2. Allosteric enzyme

3. Transition state

4. Triacyglycerol

5. Induced fit

6. Catalytic site

Answer 1

Solution:

1. Native structure of a protein is its properly folded and assembled form with operative structure and function. An unfolded protein can fold spontaneously into its native structure, based on the primary sequence.

2. Allosteric enzymes are enzymes that change their conformational ensemble upon binding of an effector, which results in an apparent change in binding affinity at a different ligand binding site. The site to which the effector binds is termed the allosteric site.

3. Transition state is the state corresponding to the highest energy along the reaction coordinate. It has more free energy in comparison to the substrate or product; thus, it is the least stable state.

4. Triacylglycerols, also known as triglycerides, are the simplest lipids formed by fatty acids. It is made up of three fatty acids ester linked to a single glycerol. Most triacylglycerols contain two or three different fatty acids. Triacylglycerols are nonpolar, hydrophobic, and insoluble in water.

5. Induced Fit - When an enzyme binds to the appropriate substrate, subtle changes in the active site occur. This alteration of the active site is known as an induced fit. Induced fit enhances catalysis, as the enzyme converts substrate to product.

6. Active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of residues that form temporary bonds with the substrate (binding site) and residues that catalyse a reaction of that substrate (catalytic site).

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