Question4 Which kind of weak interaction stabilises the two main secondary structure elements in proteins? Select one alternative: Van der Waals interactions. Covalent interactions. Electrostatic interactions between amino acid side chains. Hydrogen bonds within or between polypeptide backbones. Hydrogen bonds between amino acid side chains. ResetMaximum marks: 1 Flag question undefined

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BlackTom AI · Accepted Answer

To tackle this question, let's examine what stabilizes the two main secondary structure elements in proteins. 
Option 1: Van der Waals interactions. While these forces contribute to overall folding by stabilizing close packing, they are not the primary stabilizers of the regular recurring secondary structures like helices and sheets. 
Option 2: Covalent interactions. Covalent bonds, such as disulfide bridges, are important for tertiary structure and quaternary associations, but they do not define the repeating backbone hydrogen-bond pattern that stabilizes helices and sheets. 
Option 3: Electrostatic interactions between amino acid side chains. These ionic interactions can help stabilize certain folds, especially in tertiary structures, but they are not the hallmark stabilizers of the backbone-based secondary motifs. 
Option 4: Hydrogen bonds within or between polypeptide backbones. This is the classic stabilizing feature of secondary structure: repetitive hydrogen bonding between the carbonyl oxygen and amide hydrogen along the same backbone, leading to alpha helices (intramolecular H-bonds) and beta sheets (inter-strand H-bonds). 
Option 5: Hydrogen bonds between amino acid side chains. Side-chain hydrogen bonding can influence stability, but the characteristic, periodic hydrogen-bond network that defines secondary structure resides in backbone interactions, not side-chain H-bonds. 
Overall, the key concept is that the canonical secondary structures are stabilized predominantly by hydrogen bonds along the peptide backbone, producing the regular helical and sheet geometries observed in proteins.

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