3-1. For each of the given amino acids, write the equilib- rium reactions that would apply at a pH corresponding to each of the pK, values for each amino acid: (a) alanine; (b) glutamic acid; (c) arginine; (d) a₁, e-diaminopimelic acid (pK₁, = 1.8, pK₁₂ = 2.2, pKa, = 8.8, pK, = 9.9), whose for- a4 mula is HOOCCH(CH,) CHCOOH 1..... NH₂ NH₂
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- If the pH of a solution of Arginine is equal to a half of the 3 pka values of all of its functional groups, what will be the charge on the majority of the Arg molecules in that solution? Please explain. Am i supposedd to add up the three pka values and then divide it in half to find the pH? ThanksExplain the order of elution (with a buffer of pH 4) of the following pairs of amino acids through a column packed with Dowex 50a. aspartate before serine c. valine before leucineb. serine before alanine d. tyrosine before phenylalanineAn amino acid mixture of phenylalanine, glycine and glutamic acid is to be separated bypaper chromatography. The solvent is less polar than water. Which of these amino acids will have the highest Rf value and which the lowest? Explain. Treatment of a new protein with dansyl chloride reveals two (2) dansyl-labelled derivatives of amino acids, alanine and methionine. What can you deduce about the structure of the protein from these results? Name the amino acids that contribute atoms to both purine and pyrimidine rings.
- Chemistry Given TETRAPEPTIDE: Prolinyl-Argininyl-Cysteinyl-Tryptophan Predict the direction of the peptide in electrophoresis at pH 7 and pH11.5. (Use table on the upper right for the estimated pK values of some functional groups).Explain the order of elution (with a buffer of pH 4) of the following pairs of amino acids through a column packed with Dowex 50 a. aspartate before serine c. valine before leucine b. serine before alanine d. tyrosine before phenylalanineUsing the information below, determine the amino acid sequence of the peptide, and explain how your structure is consistent with each piece of information. Complete hydrolysis by 6 M HCl at 110°C followed by amino acid analysis indicated the presence of Gly, Leu, Phe, and Tyr in a 2:1:1:1 molar ratio. Treatment of the peptide with1-fluoro-2,4-dinitrobenzene followed by complete hydrolysis and chromatography indicated the presence of the 2,4-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. Complete digestion of he peptide with pepsin (which cleaves on the amino side of aromatic residues) followed by chromatography yielded a dipeptide containing Phe and Leu and a tripeptide containing Tyr and Gly in a 1:2 ratio.
- How many of the -amino acids shown in Table 26-1 contain aromatic rings? How many contain sulfur? How many contain alcohols? How many contain hydrocarbon side chains?Ornithine is an amino acid that is not used in the synthesis of proteins, but is an important intermediate in several metabloic pathways including the urea cycle and the synthesis of polyamines. It has a perfectly ordinary terminal amino group and terminal carboxyl group like any other amino acid (so use the pKas for those groups given on your amino acids handout), and a side chain with a single ionizable side group with a pKa of 10.3. If ornithine is placed in solution at pH 7.0, it has a net charge of +1. What would the net charge on this amino acid be if the pH of the solution was raised to pH 12.0? Please explain your reasoning.How does the shape of a titration curve confirm the fact that the pH region of greatest buffering power for an amino acid solution is around its pK's? Name four factors (bonds or other forces) that contribute to stabilizing the native structure of a protein, and describe one condition or reagent that interferes with each type of stabilizing force. Why is silk fibroin so strong, but at the same time so soft and flexible?
- The pka of ascorbic acid is 4.2 at 24C. At what pH is the ratio of the deprotonated form to the protonated form 10:1? Prove using the Henderson-Hasselback equation. How to resolve this.For the determination of Pb in blood, a 5.00 mL sample was treated with trichloroacetic acid to precipitate the proteins. After centrifugation, the resulting solution was brought to pH 3 and extracted with two 5 mL portions of methyl isobutyl ketone containing the lead complexing agent APCD (ammonium 1-pyrrolidine carbodithiolate). The extract was drawn directly into an air-acetylene flame which produced an absorbance of 0.444 at 283.3 nm. Two 5.00 mL aliquots of solutions containing 0.250 and 0.450 ppm of Pb were subjected to the same sample treatment and the absorbance that occurred was 0.396 and 0.599 respectively. Calculate the concentration of Pb in µg/dL in the blood.4b) Canavanine is closely related to arginine, and like arginine its side group has a +1 charge when protonated. If you dissolved canavanine in an aqueous solution at pH 10, what would the net charge on a molecule of canavanine be? Please show your work or make it clear how you determined the charge contribution from each ionizable group.