Draw the structure of a polypeptide backbone
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Draw the structure of a polypeptide backbone
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- Draw the resonance structure of a tripeptide peptide backbone, indicating the N- and C-terminaland give eList some of the possible combinations of α-helices and βsheets in supersecondary structures.A biochemist is designing a peptide that will form the most stable α-helix possible. He needs to synthesize an α-helix to contain a polar surface and a nonpolar surface. Assume the peptide sequence is as follows, where the numbers represent each individual amino acid in the chain. 1 – 2 – 3 – 4 – 5 – 6 – 7 – 8 – 9 – 10 – 11 – 12 The biochemist asks for your assistance. Propose a peptide sequence that would best satisfy the criteria above by providing the amino acid identity at each position (#1-12: i.e. 1-Glycine – 2-proline – 3-glycine – 4-tryptophan....). Briefly explain your design strategy by describing why the amino acids you chose are appropriate for each position (10 sentences). Make sure to include information on α-helix stability and its chemical characteristics with the properties of each amino acid chosen.
- Consider beta-sheet comprised of twelve amino acid residues (two strands of six residues each). How many hydrogen bonds should be formed between backbone atoms in this sheet?Consider an alpha-helix comprised of twelve amino acid residues. How many hydrogen bonds should be formed between backbone atoms in this helix?Draw a peptide bond between Phenylalanine (c-terminus) and Isoleucine (n-terminus).
- write the structure of the following nucleotides: 1. 5'-dGMP 2. 5'-dGDP 3. 5'-dGTP 4. 5'-GTP 5. 5'pppGpCUsing a copy of a helical wheel (attached to the end) plot the amino acids of the helix on the helical wheel. Is there any evidence of the helix as a whole being amphipathic or having a “sidedness"? Explain yes or no. Are the amino acid side chains in close proximity of one another or staggered to minimize steric hinderance between side chains? Explain the pattern you observe.What is the two factors determining the primary structure of a polypeptide chain