Long-range interactions between residues on a single polypeptide chain are classified as quaternary structures. On the other hand, interactions between residues on separate polypeptide chains are classified as tertiary structures. Both statements are correct O The first statement is correct while the second statement is incorrect Both statements are incorrect O The first statement is incorrect while the second statement is correct
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- 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 handedIndicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 10. Asp-Tyr-Lys-GIn-Thr-Ile-Phe-Met-Ser (If none of the amino acids fit the criterion, select "none".) Asp Tyr ооооооооо Lys Gln Thr lle Phe Met Ser nonebased on this oligopeptide (KEQSCMV) would someone be able to help me on the following questions? What moieties within oligopeptide are those mainly responsible for the formation of an alpha-helix? Name the process that leads to the unfolding of the alpha helix to yield a random coil. State and justify, for oligopeptide, which amino acid side chains will be involved in: hydrophilic interactions, hydrophobic interactions, disulphide bridges and salt bridges. In each case, briefly justify your choice.
- Tertiary structures refer to the three-dimensional arrangement of every atom in the molecule. On the other hand, primary structures refer to the stable arrangements of amino acid residues in a protein that give rise to recurring patterns. O Both statements are correct O Both statements are incorrect O The first statement is incorrect while the second statement is correct O The first statement is correct while the second statement is incorrectA protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown here. Only one of the Cys has a free —SH group, and the other two are involved in an —S—S— bond. The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., withdisulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the —S—S— bond (i.e., AB, BC, or AC)?Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. Lysine has three ionizable functional groups. The pKa for these groups are pK1 = 3.1, pK2 = 8.3 and pKR = 10.8. 1. Draw the structures of the predominant ionization state of Lysine at pH 1, 4, 8, and 12. Calculate also the net charge of each of these ionized molecules. Show your work. 2. Calculate the isoelectric point (pI) of Lysine in aqueous solution using the pKa values given above. Explain the rationale of your calculations and show your work.
- Which of the following statement is not true? In a secondary structure the consecutive residues have phi and psi values that are quite different. The Ramachandran diagram defines the restrictions of polypeptide backbone conformation. Two α helices with hydrophobic side chains repeated in a regular pattern can form dimeric structures in water. Greek key motifs occur frequently in antiparallel β structures. Both α helices and β sheets can be amphipathic.Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. a Histidine has three ionizable functional groups. Complete the equilibrium equations by assigning the proper pK₁ for each ionization and the net charge on the histidine molecule in each ionization state. H || H₂N-C-C-OH | CH₂ 2 + HN -1 -NH pKa = 1.8 +2 || H₂N-C-C-0- 1 CH₂ + HN -NH pKa = 9.17 Answer Bank pK₂ = 7.59 H|| H₂N-C-C-0- | CH₂ N pKa -NH = 6.0 -2 н II H₂N-C-C-0- | CH₂ +1 N C -NH 0If an oligosaccharide is attached to a protein via an O-glycosidic linkage which amino acid residue(s) are likely to be involved? O Glutamine O Serine O Histidine O Threonine O Both (b) and (d)
- The unfolding of the α helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation, a measure of a solution’s capacity to rotate circularly polarized light. Polyglutamate, a polypeptide made up of only L-Gluresidues, has the α-helix conformation at pH 3. When the pH is raised to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (L-Lys residues) is an α helix at pH 10, but when the pH is lowered to 7 the specific rotation also decreases, as shown by the following graph. What is the explanation for the effect of the pH changes on the conformations of poly(Glu) and poly(Lys)? Why does the transition occur over such a narrow range of pH?An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.Consider the peptides Pro-Gin-Val-Phe-His-Asp-Cys and His-Gln-Pro-Cys-Asp-Phe-Val. How do these two peptides differ? (Select all that apply.) The two peptides have different compositions. The two peptides have different isoelectric points. The two peptides have different titration curves. The two peptides differ in amino acid sequence. [References] If you were to have a mythical amino acid based on glutamic acid, but one in which the hydrogen that is attached to the y-carbon were replaced by another amino group, what would be the predominant form of this amino acid at pH 12 if the pK, value were 10 for the unique amino group? (Select all that apply.) Both of the carboxyl groups are deprotonated. The amino acid-carries a negative 2 charge. The amino acid carries a negative 4 charge. The amino groups are in the form -NH". Both of the amino groups are deprotonated.