Final answer:The secondary structures of the zinc metallo-beta-lactamase protein are: a. β-sheet, b. α-helix, c. π-helix, and d. α-helix.Explanation:A ribbon diagram is a 3D representation of a protein's structure, where the backbone of the protein is shown as a ribbon, with the secondary structures labeled. In this diagram, we can clearly see the presence of four types of secondary structures: β-sheet, α-helix, π-helix, and α-helix.Starting with the β-sheet, it is represented by two arrows pointing in the same direction, connected by a line. This structure is formed by adjacent strands of the protein's backbone, with hydrogen bonds between them. The β-sheet is a rigid structure that provides stability to the protein.Next, we have the α-helix, which is represented by a spiral or coiled structure. This structure is formed by a single strand of the protein's backbone, which is twisted into a helix shape. The α-helix is also stabilized by hydrogen bonds between the amino acids in the chain.Moving on to the π-helix, it is represented by a curved line, similar to the α-helix. However, in this structure, the helix is twisted in a different direction, giving it a more curved appearance. Like the α-helix, the π-helix is also stabilized by hydrogen bonds.Lastly, we have another α-helix, which is represented by a spiral or coiled structure similar to the first one. This structure is formed by a different strand of the protein's backbone, which is also twisted into a helix shape. The presence of two α-helices in this protein indicates its importance in providing stability and functionality.In summary, the ribbon diagram of the zinc metallo-beta-lactamase protein shows the presence of four secondary structures: β-sheet, α-helix, π-helix, and α-helix. These structures play a crucial role in maintaining the protein's structure and function....

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