b) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding involving the peptide bond. Describe what is going on to further stabilize secondary structure through these interactions.

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**Transcription for Educational Website:**

**Text:**

b) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding involving the peptide bond. Describe what is going on to further stabilize secondary structure through these interactions.

**Figure 1:**

Secondary interactions involving the main chain. 

- **(A)** Structural model of an idealized β-sheet, showing conventional main-chain hydrogen bonds (black dashes), C–H···O hydrogen bonds (green dashes), and C5 hydrogen bonds (blue dashes).
- **(B)** Structural model of an idealized α-helix, showing main-chain hydrogen bonds (black dashes) and \( n \rightarrow \pi^* \) interactions (blue arrows).
- **(C, D)** Orbital overlap that underlies formation of \( n \rightarrow \pi^* \) interactions (C) and C5 hydrogen bonds (D).

**Explanation of Graphs and Diagrams:**

- **Diagram A** depicts a typical β-sheet structure, highlighting various types of hydrogen bonding. Conventional hydrogen bonds in the main chain are shown as black dashed lines. Also illustrated are C–H···O hydrogen bonds, depicted with green dashes, and C5 hydrogen bonds, marked with blue dashes.

- **Diagram B** illustrates an α-helix structure, with main-chain hydrogen bonds represented as black dashed lines. Additionally, \( n \rightarrow \pi^* \) interactions, crucial for the helix's stability, are shown with blue arrows.

- **Diagrams C and D** focus on orbital interactions. Diagram C specifically illustrates the \( n \rightarrow \pi^* \) interaction, important for the stability of certain secondary structures. Diagram D emphasizes C5 hydrogen bonds, showcasing their role in the interaction network within the protein structure.

This set of diagrams and textual descriptions aids in understanding how various interactions, beyond traditional hydrogen bonds, contribute to the stabilization of protein secondary structures.
Transcribed Image Text:**Transcription for Educational Website:** **Text:** b) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding involving the peptide bond. Describe what is going on to further stabilize secondary structure through these interactions. **Figure 1:** Secondary interactions involving the main chain. - **(A)** Structural model of an idealized β-sheet, showing conventional main-chain hydrogen bonds (black dashes), C–H···O hydrogen bonds (green dashes), and C5 hydrogen bonds (blue dashes). - **(B)** Structural model of an idealized α-helix, showing main-chain hydrogen bonds (black dashes) and \( n \rightarrow \pi^* \) interactions (blue arrows). - **(C, D)** Orbital overlap that underlies formation of \( n \rightarrow \pi^* \) interactions (C) and C5 hydrogen bonds (D). **Explanation of Graphs and Diagrams:** - **Diagram A** depicts a typical β-sheet structure, highlighting various types of hydrogen bonding. Conventional hydrogen bonds in the main chain are shown as black dashed lines. Also illustrated are C–H···O hydrogen bonds, depicted with green dashes, and C5 hydrogen bonds, marked with blue dashes. - **Diagram B** illustrates an α-helix structure, with main-chain hydrogen bonds represented as black dashed lines. Additionally, \( n \rightarrow \pi^* \) interactions, crucial for the helix's stability, are shown with blue arrows. - **Diagrams C and D** focus on orbital interactions. Diagram C specifically illustrates the \( n \rightarrow \pi^* \) interaction, important for the stability of certain secondary structures. Diagram D emphasizes C5 hydrogen bonds, showcasing their role in the interaction network within the protein structure. This set of diagrams and textual descriptions aids in understanding how various interactions, beyond traditional hydrogen bonds, contribute to the stabilization of protein secondary structures.
Expert Solution
Introduction

Proteins are one of the major 4 biomolecules, these act as building blocks of biological tissues. Many monomer amino acid units adjoin via peptide bond linkages to form peptide chains and many peptide chains make a polypeptide that encodes for functional proteins.

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