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- 29. Amino Acid Chemistry: Using the amino acid chart provided..Ala-Lys-Cys & give the isoelectric point for the tripeptide. Table 23.2 The pK, Values of Amino Acids pk, a-COOH a-NH3* Amino acid side chain Alanine 2.34 9.69 2.17 9.04 12.48 Arginine Asparagine 2.02 8.84 3.86 Aspartic acid Cysteine 2.09 9.82 1.92 10.46 8.35 Glutamic acid 2.19 9.67 4.25 Glutamine 2.17 9.13 Glycine 2.34 9.60 1.82 9.17 6.04 Histidine 2.36 9.68 Isoleucine Leucine 2.36 9.60 2.18 $ 95 10.79 Lysine 2.28 9.21 Methionine 16 9.18 Phenylalanine 1.99 10.60 Proline 2.21 9.15 Serine 2.63 9.10 Threonine 2.38 9.39 Tryptophan Tyrosine 9.11 10.07 2.20 2.32 9.62 Valine O something else! 5.14 O 8.65 something else! 5.81 9.02 9.571. Draw the structures of two dipeptides: aspartic acid-glutamine and methionine-isoleucine with NH₂ and COOH at the amine and carboxylic acid ends. Show the abbreviations for both dipeptides using three-letter abbreviations and 1-letter abbreviations for the amino acid residues.7. Draw and give the full names of the amino acids in the following dipeptides. ČHS HN- OH CH, CH- OH CH2
- 1. Which of the following forms of lysine would you expect to predominate at low pH, neutral pH and high pH? 2. One of the 20 amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? Write the chemical structure of this amino acid at physiological pH.6. How are amino acids linked together in a protein molecule? Write the general structure of the tripeptide lys-phe-meth. Show their peptide bonds. Illustration: Label the amino acids.1. Draw the structure of Phe-Ser-Met-Glu, and indicate where the peptide bonds are.
- 2) For the following amino acids, encircle those with a net charge of -2 at high pH underline those with +2 at low pH Aspartic acid, Alanine, Arginine, Glutamic acid, Valine, Leucine, Lysine, Isoleucine1. Name and draw the structures of standard amino acids that would likely form hydrogen bonds with lysine in a protein at pH 7. For each example, show the hydrogen bonds with the lysine. Do not include the a-amino and a-carboxyl groups in hydrogen bonding since these would be involved in peptide bonds in the protein.2. Classify the following amino acids as nonpolar, polar basic, polar acidic, or polar neutral. (a) (b) (c) (d) H2N-CH-C-O H2N CH-C OH H2N-CH-C-OH H,N--CH-C-OH CH2 CH-OH CH2 CH, C=0 CH3 CH-CH3 OH CH3 229 OH
- 1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric point of the amino acids are as follows; histidine 7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.Shown below are three amino acids: H,N-CH-C-o ҫн, H,N-CH-C-o CH, H,N-CH-C-o ČH, Tyrosine Tyr Y Phenylalanine Phe F Alanine Ala A 1. Which amino acid is the least hydrophobic? 2. Which amino acid is most hydrophobic? 3. Which amino acid is intermediate? 4. Explain why (2) is more hydrophobic than (3). 5. Explain why (3) is more hydrophobic than (1).1.Here is an oligomeric protein, which has two binding sites:1)Write the formulas of side chains of amino acids which are located in binding sites and suggest two ligands,which can be bound with this protein. 2) Name the types of bonds which will be formed between the ligands and amino acids of binding sites.3)Give the definition of quaternary structure. What do you know about the properties of proteins with the quaternary structure?