Step 1: Understanding the Concept:
Green Fluorescent Protein (GFP) exhibits intrinsic fluorescence upon exposure to blue or ultraviolet light, making it a widely used marker in molecular biology.
Step 2: Detailed Explanation:
The molecular structure of GFP contains a built-in fluorophore located in the center of a \(\beta\)-barrel protein fold.
This internal fluorophore forms spontaneously during protein folding without the addition of helper proteins, enzymes, or cofactors (except molecular oxygen).
The chromophore is synthesized through an autocatalytic cyclization of three contiguous amino acid residues: Serine-65, Tyrosine-66, and Glycine-67 within the primary sequence of the polypeptide chain.
These residues undergo cyclization, dehydration, and oxidation to create the conjugated ring system that acts as the light-absorbing and light-emitting center.
This means Assertion (A) is correct because the protein functions autonomously, and Reason (R) is correct and directly explains why no external cofactor is needed.
Step 3: Final Answer:
Both statements are true and (R) provides the correct physical explanation for (A), as shown in option (A).