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- 5. Classify each of the following amino acids as polar or nonpolar and hydrophilic and hydrophobic. NH2 CH2 CH2 H2N-C-COOH H2N-C-COOH H. a. b. Polar or nonpolar: Hydrophilic or Hydrophobic:a. A tetrapeptide is abbreviated as PSQE. Write the name of the amino acid at the N-terminal end. b. A tetrapeptide is abbreviated as FRWL. Write the name of the amino acid at the C-terminal end.2. Given the data in the table, calculate the pl for the amino acid tyrosine. Amino Acid Glycine Alanine Valine Leucine Isoleucine Serine Threonine Methionine Phenylalanine Tryptophan Asparagine Glutamine Proline Cysteine Histidine Aspartic acid Glutamic acid Tyrosine Lysine Arginine pk₁ (-COOH) pK₂ (-NH3+) 2.34 2.34 2.32 2.36 2.36 2.21 2.63 2.28 1.83 2.83 2.02 2.17 1.99 1.71 1.82 2.09 2.19 2.20 2.18 2.17 9.60 9.69 9.62 9.60 9.60 9.15 10.43 9.21 9.13 9.39 8.80 9.13 10.60 10.78 9.17 9.82 9.67 9.11 8.95 9.04 PKR 8.33 6.00 3.86 4.25 10.07 10.79 12.48
- 1. 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.4. Amino acids a. Draw a generalized amino acid b. Label the functional groups that you recognize1. Classify the 20 common amino acids B. According to Polarity d. Uncharged nonpolar e. Uncharged polar f. Charged polar
- 8.ldentify each of the amino acid in the polypeptide and then name it using the 3-letter abbreviations. H2N- CH- CH- CH CH- CH- OH CH2 CH2 CH-OH CH2 CH2 CH2 Cн CH2 CH2 NH NH ENH NH21.Ala-Phe-Lys-Val-Val-Glu From the above polypeptide, what amino acid/s go/goes inside the cell after the following treatment: Chemotrypsin, thermolysin, then finally pepsin. What protein is left undigested? Write the primary structure of the undigested protein? 2.K-V-F-W-P-L-A-Y a.Chemotrypsin treatment b.Trypsin treatment c.Pepsin treatment d.Thermolysin treatment 3.Total acid hydrolysis of a pentapeptide complemented by total alkalinehydrolysis yields an equimolar mixture of 5 amino acids listed alphabetically, ala-cys,lys,phe,ser. N-terminal analysis with phenylisothiocyanate (PITC) generate PTH-ser. Trypsin digestion produces a tripeptide where N-terminal residue is cys and a dipeptide with ser as its N- terminal.Chemotrypsin digestion of the above tripeptide yields ala plus another dipeptide. A.What is the amino acid sequence of the tripeptide B.What is the amino acid sequence of the dipeptide derived from trypsin digestion? C.What is the primary structure of the original…6) Circle one amino acid in this peptide (hint: draw lines between not through atoms). Kahalalide F NH HN HO NH HN HN
- Select the two most hydrophobic amino acids. A. Leucine and Isoleucine OB. Arginine and Lysine OC Cysteine and Methionine D. Alanine and Glycine E. Glutamine and Asparagine6. b. Draw a box around the disulfide bridge in oxytocin, if present, or write "none". 7. Mark each peptide bond in oxytocin by making the corresponding line in the structure thicker or marking it with a different color. The first one is shown for you as an example (in dark orange). 8. Number the central carbon of each amino acid in oxytocin by pointing a small arrow to it or by circling the corresponding vertex in the image. Numbers 1 and 2 indicate the central carbons of the first and second amino acids of oxytocin, and are shown for you as an example. 9. Fill out the following table, listing amino acids that make up oxytocin in order, from the N terminus to the C terminus, characterizing each amino acid by the properties of its R group (side chains), and briefly indicating the reasoning for the characterization. You may consult amino acid groupings by category in the slides (or the textbook, p.49), but you must explain the reasoning for each in your own words. CO 1 AA# Abbre- Full…9. Identify the N-terminal and C-terminal amino acid in each peptide. H,N-CH-C-Ņ–CH-C-o- CH2 H CH3 ČH(CH3)2 HÑ-CH-C-Ņ-CH-C-N–CH–C-O- CH2 H ČH3 H ČH,CH,CONH, a.