The three pka values for the amino acid astrophan are: 1.9, 7.5, and 9.3. Calculate the isoelectric point of this amino acid if protonation of the group with a pka = 7.5 results in a positively-charged group.
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- Given the following information about amino acid tyrosine answer questions 1 & 2: A. O H HO OH HO HO рказ 10.1 H NH₂ CH₂OH A. NH3 С. НО 1. Which of the above forms of tyrosine will be predominant in a solution with pH 9.5? 2. Which of the above forms of tyrosine is a cation? Answers to Questions 3 & 4 should be selected from the following choices: CH₂OH Holl O OH B. NH₂ pka2 9.01 conj acid OH В. НО "OH D. HO HO H OH pka1 2.2 O H -OH CH₂OH C. NH3 HO NH₂ O HO OH D. 3. Which of the monosaccharides above is a non-reducing sugar? 4. Which of the monosaccharides above is an aldotetrose? 5. What is the main functional group in a protein? ||||OHDetermine the net charge (to the nearest integer) on the following peptide at pH 5 AND pH 12. Estimate the isoelectric point (pl) for this peptide: H2N-Leu-Gly-Lys-Glu-COOH Assume the pK,s for functional groups are: alpha-amino 6. alpha-carboxy sidechain-amino (Lys) 10.5 sidechain-carboxy (Glu) 4.2 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =6.6 O Net charge at pH 5 and 12 is 0 and -2, respectively, pl =3.1 O Net charge at plH 5 and 12 is +2 and -1, respectively, pl =7.5 O Nct charge at pH 5 and 12 is +1 and -1. respectively,. pl -4.5 2.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
- Diethylaminoethyl cellulose is a positively charged resin used in ion-exchange chromatography with a pKa is about 11. A negatively charged protein with an isoelectric point of 5.0 is applied to the column in a buffer at pH 7 and containing 0.1 M NaCl. Which of the following conditions is most likely to weaken the interaction between the protein and the resin? A Raising the pH to 8 and decreasing the NaCl to 0.05 M B Raising the pH to 8 and increasing the NaCl to 0.2 M C Lowering the pH to 6 and decreasing the NaCl to 0.05 M D Lowering the pH to 6 and increasing the NaCl to 0.2 MIndicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 10. Asp-Tyr-Lys-GIn-Thr-Ile-Phe-Met-Ser (If none of the amino acids fit the criterion, select "none".) Asp Tyr ооооооооо Lys Gln Thr lle Phe Met Ser noneCalculate the net charge of the following peptide at pH 2, pH 6 and pH 14 (use 2 and 9 as pKa values for the carboxylic acid and amino groups, respectively, use the attached table for the side chain pKa values). Ile-Leu-Ile-Lys-Glu-Cys-His-Glu-Met-Ile-Ser-Thr-Arg-Tyr
- The following amino acid is dissolved in solution at pH 7.4. HC H' + CH CH₂ H/ H+ HC a. Which amino acid is this? (all lower case) N- H CH CH₂ b. What is the pKa of its ionizable side chain? (Use the value from the textbook.) c. What is the ratio of the uncharged to the charged form at pH 7.4? (write answer as number with one decimal place, ex 2.5 or 0.2 or 50.0 with an implicit "to 1")For the following pentapeptides: Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser Draw the most protonated forms of the pentapeptides Illustrate the ionization of the pentapeptides from the most protonated to its deprotonated form. Label the ionization with its respective pK values. Compute their isoelectric pH (pI). Do these peptides with the same amino acid composition have different net charges at pH 7.0? Explain briefly. Would you expect the titration curves of the two peptides to differ? Why or Why not?The skeletal structures of the two amino acids, glycine and lysine, are given below along with the values of the relevant acid dissociation constants (pKa). NH,* PK, - 10.79 - HạN*CH2CO,¯ S pK¸=2.35 (CH2)4 - H3N*CHCO,- pK,=9,78 lysine (Lys) glycine (Gly) pK, = 9.18 pK, - 2.16 For an aqueous solution of glycine alone, calculate the value of pH at which the ratio of the concentration of neutral glycine zwitterions to the concentration of protonated cation is 102. On your under each of the following conditions. In the blank, provide the total charge of the dipeptide. (Example: If the charge is two plus write the answer simply as 2, if the charge is negative two write the answer as -2). draw the skeletal structure of the dipeptide, Lys-Gly, when it is solvated in an aque us solution i. pH= 1 ii. pH= 12
- Amino acids, such as glycine, are the key building blocks of proteins and will be discussed in greater detail in Chapter 25. At the pH of the stomach, glycine exists predominantly in a protonated form in which there are two acidic protons of interest. The pKa values for these protons are shown. Using this information, draw the form of glycine that will predominate at physiological pH of 7.4.The amino acid arginine ionizes according to the following scheme: NH₂ I C=N I ΝΗ Part A pl = Submit H (CH₂)3 H-N-C-COOH II HH 1 [ΠΙ ΑΣΦ H H Calculate the isoelectric point of arginine. Express your answer using three significant figures. Request Answer pk-2.17 -H* +H* wwwww NH₂ C=N ΝΗ H (CH₂)3 1 ? H H-N-C-COO- | | H H 11 H pk-8.99 -H* +H* NH₂ I C=N I ΝΗ T (CH₂)3 H H H₂N-C-COO- I H pk - 12.5 -H* +H* NH₂ C=N=H NH I (CH₂)3 H₂N-C-COO- I H IVWhat is the net average charge on the predominant form of lysine at pH values of (a) 2.0, (b) 5.0 and (c) 7.0? CLUE: draw the structure of lysine and show its different charged forms; then consider in which pH domains the pKa values for deprotonation/protonation occur.