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- Shown below is the structure of a polypeptide with the pK, values of its acidic hydrogens. pK = = 10.1 H OH pK, = 9.2 H. pKa = 2.1 H. N-H pK, = 6.0 pKa = 3.9 1. How many peptide bonds are present in one molecule of the polypeptide? [ Select ] II. Over what pH range would this molecule predominantly exist in a state that has a net charge of zero? [ Select ] ZIfirst amino acid is R second amino acid is L Draw your dipeptide at pH 7.4 What is the Log Kow of the pesticide What is the molar concentration in the octanol phase What is the number for the pesticide How many chiral centers does your assigned pesticide contain?Make use of the table below in answering the questions asked: Amino acid pK₁ pK₂ pK, Isoleucine 2.32 9.76 Leucine 2.32 9.74 Lysine 2.16 9.06 10.54 Tyrosine 2.20 9.21 10.46 1. Kindly draw manually the structure of tripeptic ILY at pH 7.00 2. Kindly draw manually the most protonated structure of tripeptide ILY
- Consider the tetrapeptide C-A-F-E Draw the structure of the tetrapeptide at pH 1.3. What is its charge at this point? Draw the structure of the tetrapeptide at pH 8.2. What is its charge at this point? Draw the structure of the tetrapeptide with 0 net charges. What is its pL?Match each charge form of alanine under the pH condition where it would be the predominant form. The pka values for the carboxyl group and amino group of alanine are approximately 2.3 and 9.7, respectively. H H H Н.С — с — соо H Н.С — с — соо Н.С— с —соон Нс — с —соон NH, NH, NH NH, A B D v pH11 2. A Does not occur in significant amounts at any pH 3. D 4. B1. 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?
- 6. Using the charges you calculated above, plot the characteristics of alanine over a range of pH values. Connect the points by estimating what the charge should be at pH values where you lack data. It is possible to calculate the charge at any pH, but if you understand the relationships presented here you will be able to make estimates quickly and easily. +2 +1.5 +1 - +0.5- -0.5 - -1- -1.5 - 7. 6. 11 13 14 pH of solution 7. Aspartic acid has a side chain bearing a carboxylic acid group; its pK, is 4. The a-amino and a-carboxylic groups have pKa values similar to those of alanine. Determine the net charge on aspartic acid at the following pH values: pH 1 pH 2 pH 4 pH 9 pH 13 Net charge of molecules 2.1. 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.1. Cysteine is an important amino acid that stabilizes the structure of peptides and proteins by the formation of disulfide bond with another cysteine residue. Illustrate the titrimetric profile of cysteine and calculate its isoelectric pH. [Hint: The sulfhydryl group is titratable] 2. The tripeptide Glu-Pro-Arg (EPR) which is a product of Lactobacillus casei fermentation of milk was found to have potent blood pressure lowering properties. Draw the structure of the tripeptide, give its systematic name, show its titration profile, and determine its isoelectric pH.
- Solve the peptide problem. 1. Write the structure of tripeptide in which the first amino acid is Trp, the second one is Glu, and the third one is Asp. Mark its N- and C-ends. What is the pl area of the tripeptide (>7)? Explain. What is the charge of the tripeptide placed in a buffer solution with pH 9,2? Explain. How do you think, would the Xanthoprotein reaction be positive in the solution of this peptide? Explain.1. Draw the structural formula of the amino acid valine that predominates in solution at each of the following pH values. А. рH 3D7.0 В. рH %3D 12.0 С. рH %3D 2.0 2. Draw the structural formula of the amino acid phenylalanine that predominates in solution at each of the following pH values. А. рH%3D 3.0 В. рH %3D 10.0 С. рH%3D 7.0The pka of the side chain of histidine is 6.00. What is the percent of protonated histidine at pH 6.4? 15.3% 28.5% 45.3% O 66.6%