Concept explainers
(a)
Interpretation:
The titration curves for the reaction of glutamic acid with
Concept Introduction:
In the titrations of amino acids, the most acidic group
(b)
Interpretation:
The titration curves for the reaction of histidine with
Concept Introduction:
In the titrations of amino acids, the most acidic group
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Organic Chemistry
- Draw the resonance forms of a protonated guanidino group, and explain why argininehas such a strongly basic isoelectric pointarrow_forwardGiven pKa values for ionizable groups from Table 27.2, sketch curves for the titration of Q.) glutamic acid with NaOHarrow_forwardCalculate the overall yield of bradykinin when the yield for the addition of each amino acid to the chain is 70%.arrow_forward
- Sketch a titration curve for the following amino acids and indicate the pKa values for all titratable groups. Also indicate the pH at which this amino acid has no net charge. lysine aspartic acidarrow_forwardGlycine solution was titrated against NaOH and pH of the final solution was 4.8. Given that the pKa¹ and pKa² of glycine are 2.34 and 9.60, respectively. Calculate the concentration of the dissociated amino acid in terms of the undissociated amino acid, if [x] and [y] are the concentrations of dissociated and undissociated amino acid, respectively.arrow_forwardWhy is the side chain Pka of amino acid so much higher ?arrow_forward
- Sketch a titration curve for the following amino acids and indicate the pKa values for all titratable groups. Also indicate the pH at which this amino acid has no net charge.a. cysteineb. lysinec. aspartic acidd. gly-varrow_forward1.Whatare ampholytes 2. What is zwitterion 3. Under what cincondit do zwitterion exist 4. What happens when a zwitterion is titrated with an acid 5. Under what condition will an amino acid have a Pka 6. Draw the structure of Glycine as zwitterionarrow_forwardOne of the drawbacks of older methodology for nonprotein testing was that ________________, which modern methods have corrected for. Question 2 options: A) a protein-free filtrate needed to be made B) it was difficult to separate BUN from creatinine C) ammonia was too volatile D) substrate was a limiting factorarrow_forward
- The biruet method uses what reaction to quantify total protein in serum? Question 4 options: A) Cupric ions + peptide bonds in alkaline medium --> violet colored chelate B) Ferric ions + carboxyl bonds in alkaline medium --> aqua colored chelate C) Cupric ions + carboxyl bonds in acidic medium --> aqua clored chelate D) Nitrogen determined via titration with HClarrow_forwardIf 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? Thanksarrow_forwardIf a mixture of Glu (pI=3.22) and Arg (pI=10.76) is passed through a cation exchange column at pH=7.0, we would expect Glu to elute first and arginine to stick to the column. A. True B. Falsearrow_forward
- Introduction to General, Organic and BiochemistryChemistryISBN:9781285869759Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar TorresPublisher:Cengage Learning