Which of the following is true regarding alpha-helix and beta-sheet? The formation of a beta-sheet does not involve hydrogen bonds. For transmembrane proteins, the amino acids in the transmembrane segments only have polar side-chains. The backbone amino group of every amino acid in an $\alpha$-helix form a hydrogen bond with backbone carbonyl group of the amino acid two positions away. The amino acid side chains extend away from the center of the alpha-helix.
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The question asks to identify the true statement among the given options regarding alpha-helix and beta-sheet structures in proteins. Show more…
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4. The secondary structure of proteins is made of a few characteristic patterns that occur frequently within folded proteins. These recurring shapes, which are particularly stable, are named ̑̑-helix and ̑̑-sheet. Which of the following statement about ̑̑-helices and ̑̑-sheets is wrong? (a) ̑̑-helices and ̑̑-sheets are stabilized by hydrogen bonds forming between the amino and carbonyl groups in the polypeptide backbone. (b) In an ̑̑-helix, the helix makes a complete turn every 3.6 amino acids. (c) ̑̑-sheets can be called parallel and anti-parallel. (d) The nature of the amino acid side chain is important for the folding of ̑̑-helices and ̑̑-sheets. (e) A segment of an ̑̑-helix composed of nonpolar amino acids can span a membrane bilayer.
Adi S.
36. A protein whose peptide backbone is mostly extended and hydrogen bonded to different strands of the protein is mostly composed of the secondary structure. 37. In an alpha-helix, the side chains on the amino acid residues: 38. Which one of the following is NOT a tertiary interaction in proteins?
Which of the following statements about β-sheet structures is true? Parallel β-sheet structures have backbone amides that directly hydrogen bond between strands, whereas antiparallel β-sheets have hydrogen bonds that are offset. The individual strands of all β-sheet structures are connected by turns, helices, or loops. All amino acid side chains in antiparallel and parallel β-sheet structures point to one side of the sheet. All β-sheet structures form a spiraling backbone chain.
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