Why pl (isoelectric point) of amino acid with acidic or basic side chains is the average of the two pka values that correspond with the similar group? Give your explanation.
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- A 100 ml solution of 0.1 M amino acid (AA) at ph 1.0 was titrated with NaOH solution. The pH was monitored, and the results were plotted on the graph. The keypoints in the titration are designated I to VII. What is the possible identity of the amino acid? What is the isoelectric point of AA? what is the pKa corresponding to the dissociation of the alpha carboxylic group? Region/point where AA is predominantly present as a (-1) charged species? The effective buffering range for the amino acid in the acidic region? Region/point where the solution has 50:50 percent mixture of the (0) and (-1) speciesConsider an amino acid (A) with no ionizable side chains, and call the three species involved in the acid/base equilibria H2A+, HA, and A- (see scheme below). Assume that pKa(1) = 2.0 and that pKa(2) = 9.0. Suppose that the total concentration of the amino acid is 1.0 mM. Report to two significant digits. pH [H2A+] (mM) [HA] (mM) [A-] (mM) 1.0 2.0 3.0 4.0 5.0 6.0 7.0 8.0 9.0 10.0 11.0 12.0Amino acid Cys has ionizable groups with pKa values 2.0, 8.0, and 10.0. Determine the charge on the Cys at the following pH. Be sure to write the charge in fraction with sign in front (for example, +1/2, -1/5, and +7/8). Charge when pH is at 1.0? _________ Charge when pH is at 9.0? _________ Charge when pH is at 8.0? _________ Charge when pH is at 10.0? _________
- The simple average molecular weight of the 20 common amino acids is 138 , but most biochemists use 110 when estimating the number of amino acids in a protein of known molecular weight. Why do you suppose this is? (Hint: There are two contributing factors to the answer. One of them will be apparent from a brief consideration of the amino acid compositions of common proteins. See, for example, Figure -Bellow)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.Histidine is an amino acid containing an ionizable group in its side chain. This ionizable group has a pka of 6.0, meaning that His is in its deprotonated form at physiological pH (7.0-7.4). However, His is included in the positively charged amino acid category. Calculate the ratio of deprotonated/protonated His at pH 7.0, and use your answer to justify why this amino acid is included in the positively charged amino acid category. Show all work for full credit.
- To calculate the isoelectric point of amino acids having other ionizable functional groups, we must also take into account the pk, of the additional functional group in the side chain. For an acidic amino acid (one with an additional acidic OH group): For a basic amino acid (one with an aditional basic NH group): pK, (a-COOH) + pK, (second COOH) - pKa (a-NH3") + pK, (side chain NH) pl = a. Indicate which pK, values must be used to calculate the pl of each of the following amino acids: [1] glutamic acid; [2] lysine; [3] arginine. b. In general, how does the pl of an acidic amino acid compare to that of a neutral amino acid? c. In general, how does the pl of a basic amino acid compare to the pl of a neutral amino acid?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.You have a peptide that has the following amino acid sequence: GPMG Draw the structure of the polypeptide's most protonated form, and its charge. Then draw the structures of the increasingly deprotonated forms, along with their charges. Use the information from these structures to calculate the pl (isoelectric point) of the peptide using the pKa values provided in the table below. Write the pl as x.yz, for example, 7.62 or 3.09. Group Terminal a carboxyl group Aspartic acid Glutamic acid Histidine Terminal a-amino group Cysteine Lysine Tyrosine Arginine Acid EM 2-0" + H -N H H N-H H N-H T Base 1 1. تر H -5 H H O™ N-H Typical pK, 3.1 4.1 6.0 8.0 8.3 10.8 10.9 12.5
- Given the following Peptide: Q6 *H;N-Phe-Asp-Ala-Arg-Gy-His-Arg-Asp-Glu-His-Tyr-CO 6a. What is the peptide's net charge at pH 2.0, pH 6.0, pH 7.4, and pH 10.2? (show work) 6b. What is the approximate isoelectric point of this peptide?how does the protein environment surrounding an amino acid chain affect its chemical properties?Consider the carboxyl group on an asparate side chain in the following environments in a protein. Rank in order these environments from the highest to the lowest proportion of carboxyl groups in the -COO- form.that is in terms of pKas. 1. an aspartate side chain on the surface of protein with no other ionizable groups nearby. 2. an aspartate side chain buried in a hydrophobic pocket on the surface of a protein 3. an asparate chain in a hydrophobic pocket adjacent to a glutamte side chain 4. an asparate side chain in a hydrophobic porket adjacent to a lysine side chain.At which pH would the peptide with the amino acid sequence 'KEYHR' be found in an IPG (Immobilized pH gradient) strip after successful isoelectric focusing. Show calculation. lonizable groups Alpha amine group of K Side chain group of K Side chain group of E Side chain group of Y Side chain group of H Side chain group of R Alpha carboxylic acid group of R pka 8.95 10.53 4.25 10.07 6 12.48 2.17