What does the "alpha" indicate in "α-helix"? It is a Greek helix. It's position lies above the beta-pleated-sheet. It has only the one enantiomer. It predominates in the 3º structure of the protein. None of these.
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What does the "alpha" indicate in "α-helix"?
It is a Greek helix.
It's position lies above the beta-pleated-sheet.
It has only the one enantiomer.
It predominates in the 3º structure of the protein.
None of these.
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Solved in 3 steps
- 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.A helical wheel is a two-dimensional representation of a helix, a view along its central axis. Label the blanks on the helical wheel diagram to show the distribution of amino acid residues in a helical segment with the sequence -Val-Asp-Arg-Val-Phe-Ser-Asn-Val-Cys-Thr-His-Leu-Lys–Thr-Leu-Gln-Asp-Lys- 1 Answer Bank H L D K R F T K S TIt is often the case that a helices are positioned in a protein such that one side faces the interior of the protein and the other, the surface of the protein. These are said to be amphiphilic helices because they face different environments. Using a helical wheel projection (shown below), which of the peptide(s) below might form an amphiphilic helix? 8 15 1 12 4 11 16 18 9 7 14 13 10 17 O SLIKSVIEMVDEWFRTFL O FLIRVLRKVFRVLTRILS O RLFRSRVLKIAVIRFLLI
- Which statement is true regarding an a helix, there are five residues per helical turn. the helix is right-handed there are usually many proline residues present. side chain residues point up and down the axis of the helix.Proline is known as a beta sheet and alpha helix "breaker ," therefore proline is rarely found in beta sheets or alpha helices. why do you think this is? In your explanation, you should describe the specific molecular interactions necessary for the formation of alpha-helices and beta-sheets. Please be as specific as possible.The pi-helix is a rare secondary structural element in proteins that resembles an alpha helix but has slightly different properties. Notably, hydrogen bonds within a pi-helix display a repeating pattern in which the backbone C=O of residue i hydrogen bonds to the backbone HN of residue i+5. Based on this information, which of the following are true? Select all that apply. O The hydrogen bonding distance between C=O and NH groups remains unchanged between pi-helices and alpha-helices The torsion angles of amino acids found in pi-helices are the same as those found in alpha-helices Pi-helices have a smaller rise per residue compared to alpha- helices Pi-helices have fewer residues per turn compared to alpha-helices Pi-helices have more residues per tůrn compared to alpha-helices Pi-helices are left handed
- This cartoon represents the quaternary structure of proteins and each color of the different shape represents a different subunit. 1. How many N-terminus are there in this cartoon?In 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-ValWhich of the following amino acids is most unlikely to be present in a beta sheet? Lysine Valine Leucine Isoleucine 14
- How can a protein’s potential function be determined from a protein’s primary structure? I assumed this was not possible, I thought its function was determined from its 3-dimensional structure only. Thank you for explaining this.This image shows the tertiary structure of a protein segment. Tertiary structure results from different interactions, or forces, between groups. Move the example of each force to the appropriate description on the protein. Then, identify the major force controlling tertiary structure. (Need help) It says I'm wrong.Glutamine is a conservative replacement for asparagine in the primary structure of a protein. This implies that
