If the polypeptide chain GHREAQNF were in an alpha helix, then the alpha am group of amino acid N would be in a hydrogen bond with the C=O of Please write letter of amino acid as answer.
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The alpha helix of a protein structure is a type of regular secondary structure where successive amino acids adoptsimilar Phi and Psi dihedral angles.
It is a right-handed helix with all the peptide bonds located on the inside, while the side chains extend outward.
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- Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.Draw the oligopeptides' structure and provide the corresponding name for each oligopeptide 1. Dipeptide Ala-His 2. Tripeptide Glu-Pro-Cys Note: First residue is the N-terminal amino acidDraw out the structural formula of the oligopeptide, with the first amino acid as the N-terminus
- Consider an alpha-helix comprised of twelve amino acid residues. How many hydrogen bonds should be formed between backbone atoms in this helix?At neutral pH, which of the following amino acids has a net positive charge, which has a net negative charge, and which is neutral? (Hint: Draw the various charged forms of each amino acid before deciding.)(a) Aspartic acid (b) Histidine (c) ValineIn the following polypeptide, which amino acid would be participating in hydrogen bonding with alanine, given this sequence forms an alpha helix? Please write out the full amino acid name, not the abbreviation. Met-Ala-Leu-Glu-Lys-Thr-Leu-Val
- Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys CysI-D-E-L-Y-S-Q-V-C-S-H-L-D-T-V-R This amino acid sequence forms an alpha helix. When thinking about how the helix folds into its tertiary strucutre, use entropy and enthalpy to explain what would happen energetically.The primary amino acid sequence of a stretch of polypeptide is Asp-Glu-Pro-Lys-His-Arg. Would you expect this portion of the polypeptide to form an alpha helix at pH=5? Provide 3 reasons to justify your answer.
- The structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond towards the C-terminal end of the helix while the hydrogens of the NH groups orient toward the N-terminal end, thus imparting a dipole along the length of the helix. As a result, which kinds of amino acids would favor the C-terminal end, and which would favor the N-terminal end? negatively charged, positively charged positively charged, negatively charged negatively charged, hydrophobic positively charged, hydrophobic hydrophobic, negatively charged hydrophobic, positively chargedWhich of the following is/are least likely to be found in an alpha helix because it has an inappropriate Phi angle. a Polar charged amino acids b Proline c Nonpolar amino acids d Glycine e Polar uncharged amino acidsConsider 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?