2. Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal –NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0.
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- 1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation1. Draw the structures of the 20 biologically active AA. Under each structure, write the name, one-letter code, and three-letter code followed by the AA classification based on polarity.1. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 7? 2. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 12?
- 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?4. What is the region/point where AA is predominantly present as a (-2)-charged species?5. The effective buffering range for the amino acid in the acidic region is?6. What is the region/point where the solution has a 50:50 percent mixture of the (0) and the (-1) species?A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…
- 1. a. Explain why the melting point of palmitic acid (16 carbons, no double bonds) is slightly lower thanthat of stearic acid (18 carbons, no double bonds). Explain why the melting point of oleic acid (18carbons, one double bond) is lower than that of stearic acid b. A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.1. Methionine is an amino acid that contains a ___. *a. sodium atomb. sulfur atomc. phenyl ringd. heterocyclic ringe. chlorine atom 2. Which of the following shows all of the tripeptides that can be formed from one molecule each of glycine (Gly), valine (Val), and leucine (Leu)? *a. Gly-Val-Leu, Gly-Leu-Val, Leu-Gly-Valb. Val-Gly-Leu, Gly-Val-Leu, Gly-Leu-Val, Leu-Gly-Valc. Gly-Val-Leu, Gly-Leu-Val, Val-Leu-Gly, Val-Gly-Leu, Leu-Gly-Val, Leu-Val-Glyd. Val-Gly-Leu, Gly-Leu-Vale. Gly-Val-Leu 3. Two amino groups are present in ___. *a. leucineb. Lysinec. Glutamic acidd. threonine1.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?
- 1. Choose the proper structure of the predominant form of L-M-L-P-D-T at pH 5. Provide a short explanation. 2. Choose the proper structure of the predominant form of L-A-L-Y at pH 11. Provide a short explanation.1c) Suppose you increased the pH of the biotin solution from 7.0 to 9.0 -what would happen to the ionizable group on a molecule of biotin as the pH shifted from 7.0 to 9.0?1. Which peptide would be more soluble at pH 7.0, (Val)₂₀ or (Asp)₂₀ ? at pH 3.0, (Gly-Glu-Val)