Final answer:
A protein crystallized to reveal a beta barrel structure is likely involved in transport or pore formation, often found in membranes of bacteria, mitochondria, or chloroplasts, and is critical for molecular passage through membranes.
Step-by-step explanation:
If you crystallize a protein and determine that it is comprised of a series of beta strands arranged into a beta barrel, this protein is most likely to be involved in functions such as transport or pore formation within cell membranes. Proteins with beta barrel structures are often found in outer membrane proteins of Gram-negative bacteria, mitochondrial membranes, and chloroplasts. These beta barrels are formed by beta sheets that curve around to close upon themselves, creating a barrel-like structure. This structure allows for a hydrophilic pore to form, which can be essential for molecules to pass through otherwise impermeable membranes.
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The arrangement of beta sheets in the protein's secondary structure can either be parallel or antiparallel, forming hydrogen bonds that stabilize the overall structure. Given the importance of the tertiary structure in determining the protein's function, a beta barrel likely indicates a protein that interacts with other biological molecules, facilitates transport across a membrane, or contributes to the structural integrity of cellular components.