Explain, what role can a minor conformer (1% of the total protein conformational

Question

Explain, what role can a minor conformer (1% of the total protein conformational species) play for the activity of an enzyme? In other words, if 99% of the protein molecule belongs to the "native fold", why and how could the remaining 1% be relevant for its function? For three spectroscopic methods- Fluorescence, UV spectroscopy, Solution NMR spectroscopy-explain if the technique can or cannot be used to probe the minor (1%) conformational species and why. Fluorescence UV spectroscopy Solution NMR spectroscopy

Explanation / Answer

* A minor conformor mediates functions like interaction with ligand, enzyme activity. Minor conformors contain the active site of an enzyme. Amino acids which are spaced far away from each other in their primary structure are brought close together to form a pocket called active site. The amino acids that catalyze a reaction are spatially oriented in a way that facilitates the reaction.

The rest of the protein molecule makes the native fold. Though only few amino acids actually participate in catalysis (in the active site), the entire protein structure is necessary for this catalysis. The three-dimensional strucutre formed by the protein creates a mileu suitable for catalysis (for example, the 3-D fold may exclude the chance of any other nucleophile in the pocket, except the amino acids in the catalytic site, so that the substrate can be made a nucleophilic attack).

This can be compared to our palm and fingers, and rest of the hand. Though we do most of our works with our fingers and palm, the entire hand is necessary for proper projection and orientation of the palm to accomplish the tasks. Imagine how you work if you dont have a hand, and the palm is attached to the shoulders. The native fold creates the flexibility, local environment, and conformation that enables the active site to function.

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