Please solve **Understanding Protein Structure and Interactions**Proteins have complex three-dimensional structures. These polymers are held into these specific shapes with a variety of intermolecular forces, covalent bonds, and ionic bonds. Proteins fold into complex tertiary shapes that are held in place with a variety of attractive forces.Identify the type of interaction depicted in the diagram below:![Diagram of Protein Interaction](diagram-placeholder)- **A)** ion-ion bonds- **B)** disulfide bonds- **C)** hydrogen bonding between functional groups on amino acid residue side chains- **D)** hydrogen bonding between the carbonyl and NH of the backbone of the protein- **E)** hydrophobic interactions (London Dispersion forces) between nonpolar amino acid residue side chains*Correct Answer: C) hydrogen bonding between functional groups on amino acid residue side chains*### Explanation of the DiagramThe diagram illustrates two amino acid residues interacting through hydrogen bonding. The interaction is critical in maintaining the protein's tertiary structure. The blue curved lines indicate the presence of the hydrogen bonds, a type of attractive force resulting from the interaction between a hydrogen atom attached to an electronegative atom (like oxygen or nitrogen) and another electronegative atom.This type of bonding is essential for the stability and functionality of proteins, as it helps to hold the folded shape of the protein by bonding side chains of the amino acids. Understanding these interactions is crucial for comprehending how proteins attain their functional configurations.

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Proteins have complex three-dimensional structures. These polymers are held into these specific shapes with a variety of intermolecular forces, covalent bonds, and ionic bonds. Proteins fold into complex tertiary shapes that are held in place with a variety of attractive forces. Identify the type of interaction depicted here. H₂N A) ion-ion bonds B) disulfide bonds C) hydrogen bonding between functional groups on amino acid residue side chains D) hydrogen bonding between the carbonyl and NH of the backbone of the protein E) hydrophobic attractions (London Dispersion forces) between nonpolar amino acid residue side chains