4. Which of the following amino acids has an imino ring? A. Proline B. Tyrosine C. Tryptophan D. Histidine
Q: 1. For the nucleotide shown below, answer the questions below. NH, N. N. -0-P-O-CH, 0- H H H ОН OH
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Q: . Which type of proteins are also known as denatured proteins? A. Primary proteins B. Secondary…
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Q: 3. An alteration of genetic information is shown below. A-G-T-A-C-C-G-A-T → A-G-T-G-A-T What type of…
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Q: 8 What are the three components of anucleotide?
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Q: 7. A proteolytic enzyme has the following action:
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Q: 6 What is the complement of the mRNA triplet code in the tRNA? 7 In what way is tRNA different from…
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Q: 4. Which among the given peptides will form hydrogen bond with another similar peptide chain? i.…
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Q: 4) Using the pK, data found in the supplied chart, determine the predominant charge of each amino…
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Q: 10. Which of the following is a purely ketogenic amino acid? A. Tyrosine B. Leucine
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Q: 7. What type of bond is formed between the hydroxyl group of one nucleotide and the phosphate group…
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Q: Draw the structures of the amino acids tyrosine and aspartic acid
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Q: 2. Which of the following forms of lysine would you expect to predominate at low pH, neutral pH, and…
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Q: 8. Chaperones is/are useful in: a. Folding of protein b. Release of protein c. Denaturation of…
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Q: Draw three-dimensional representations of the following amino acids.
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Q: 3. What are the functions of lysine in human health?
A:
Q: 6. Which of the following acts as lipid-soluble radical trapping antioxidants? A. Ascorbate B. Uric…
A: There are two types of radical trapping antioxidants:- Water soluble lipid soluble
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Q: 3. Polar amino acids is/are: a. Serine b. Tryptophan c. Tyrosine d. Valine е. Lysine
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Q: 1. Which one of the following statements concerning the peptide shown below is correct?…
A:
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Q: 5. What mutation(s) would eliminate peptide translation? Nonsense mutation
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A: The explanation for the wrong statement is given below.
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Q: 3. Which of the following is not a nitrogen base found in DNA? O Thymine Guanine Adenine Uracil
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Q: 3. Fill in the missing molecules or required cofactors. PLP b) @NH₂ OH
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Q: 1. Which of the following is a weak base? A. CH,COOH B. CH;CH;NHCH, C. HOCN D. NAOH E. None of…
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- 1. Show the Dehydration Synthesis reaction that occurs to form a dipeptide containing the following amino acids: i) cysteine and serine leucine and lysine1. What will happen if there is a change in the configuration of a protein molecule? Provide an example. 2. Give the IUPAC name for Ala-Gly-Leu1. H3N a. Draw the peptide sequence, including stereochemistry (wedges and dashes) for Glu-Cys- Gly. The N-terminus is drawn for you as a starting point.
- 1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?2. Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show in zig-zag style, from amino to carboxy terminus, with correct stereochemistry a. Draw the predominant form at pH = 2 b. Draw the predominant form at pH = 5 c. Draw the predominant form at pH = 7 d. Draw the predominant form at pH = 121. What is the isoelectric point of tyrosine? Draw out the different structures of tyrosine at each pka. 2. Draw the tripeptide containing Ser-Ala-Val.
- 9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin.3. List down the isomers of the tripeptide Ala-Cys-Lys.2. Come up with a synthesis strategy to make the dipeptide ser-asp. To do this you will need to provide a lot of information. a. Synthesis schemes starting from unmodified the amino acids, ser and asp, including:1. Initial protection of the amino acids2. Coupling of the amino acids using PyBop3. Deprotection of the N and C termini
- 1. a. Draw the following pentapeptide: lysine-leucine-aspartate-threonine-phenylalanine b. Label the amino and carboxyl terminus of your peptide c. Label each amino acid residue with one and three letter abbreviations d. Label the alpha carbons e. Label the bonds around which phi and psi rotational angles occur f. Which amino acid in this chain is most likely to be phosphorylated? Which amino acid is most likely to be acetylated?Asparagine belongs to amino acid that are classified as O a. positively charged O b. polar uncharged O c. negatively charged O d. hydrophobic4. Draw the following amino acids linked by peptide bonds: a. aspartate b. lysine c. cysteine d. tryptophan Indicate the letter designation for each amino acid.