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Concept explainers
(a)
Interpretation: In an
Concept introduction: The arrangement of the portion of protein backbone in space gives the secondary protein structure. There are two types of secondary structure, the alpha helix and the beta pleated.
(b)
Interpretation: In an
Concept introduction: The arrangement of the portion of protein backbone in space gives the secondary protein structure. There are two types of secondary structure, the alpha helix and the beta pleated.
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Chapter 20 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- a. Classify tertiary structures of proteins and give one example from each class. b. In their tertiary structures some proteins are known to fold into specific nativa conformations. Discuss protein folding and the forces stabilizing them. A Paragraph В I 国 回arrow_forwardThe primary structure of a protein is shown below. Please answer the following questions. Leu-Arg-Ser-lle-Glu-Thr-Val-Val-Asn-Gln-Val-lle-Ser- Tyr a. Where is this section of the polypeptide most likely located [ Select ] completely embedded inside the protein partially exposed to the aqueous environment b. Is the above more likely an alpha helix or a beta-pleated sh completely exposed to the aqueous environment c. Which two amino acid residues are least likely to be in an alpha helix, but most likely to be a part of a beta turn? (Please select the amino acids in alphabetical order). [ Select ] [ Select ]arrow_forwardLoop regions play important roles in the secondary structure of protein. Define loop region and give three (3) of the rolesarrow_forward
- A. Write the structure of the following peptide at pH 5.0 and calculate its net charge at this pH. Asp-His-Tyr-Arg-Lys-Leu-Thr-Gln. Based on the pKa value of the ionizable groups. B. A polypeptide consisting only of L-glutamate residues (poly-L-glutamate) may have a random coil or helical structure depending on pH. Explain this behavior by indicating at what pH values the helical structure will be favored.arrow_forwarda.Describe the bonds which hold a quaternary protein molecule together. b. Discuss the reasons why glycine and proline are not usually found in an alpha helix of proteins.arrow_forwardDraw the chemical structure of an alanine pentapeptide. Indicate the location of each peptide bond. Label the phi () and psi () dihedral angles. Name and briefly define the four levels of protein structure.arrow_forward
- Using 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.arrow_forwardsay you have been asked to determine the molecular structure of a soluble protein with roughly 500 amino acids per subunit. you think there may be a lysine and aspartic acid interaction so but you want to get molecular conformation. what structural technique would you utilize in order to picture this interaction and what resolution would be needed?arrow_forwarda) Canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do are other intermolecular interactions important to fully understand folding processes?arrow_forward
- Suppose that the given peptide below is a segment in a globular protein's primary structure. Determine what would most likely be the type of secondary structure that it will form. Explain. T-L-S-A-R-I-D-Varrow_forwardName another condition besides heat and exposure to a bond disruptor (like alcohol) that could affect the ability of a protein to maintain its shape. Explain.arrow_forwardThe 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 handedarrow_forward
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