Interpretation:
The most acidic hydrogens present in the given compound should be identified.
Concept introduction:
Strong Acids: Acids that dissociates into ions completely which results in easy donation of protons are considered as strong acids. Strong acid forms weaker conjugated base.
Weak Acids: Acids that do not easily dissociate into ions completely which has difficulty in proton donation are considered as weak acids. Weak acid forms stronger conjugated base
Electrostatic potential map: It is 3D representation of molecules which shows the distribution of charges present in the molecule. Generally red, orange, yellow, green and blue defines the charge potentials present in the molecule.
The blue color indicates the most positive potential end and the red color defines the most negative potential end.
Want to see the full answer?
Check out a sample textbook solutionChapter 10 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- Write equations to show the ionic dissociationreactions of the following amino acids: aspartic acid, valine, histidine,serine, and lysine.arrow_forwardThe order of elution of amino acids X, Y, VW and Z in a cation exchanger eluted with a buffer of increasing pH is as follows: Z, W, Y, X (last). If the amino acids are glutamic acid, arginine, phenylalanine and alanine, what amino acid can Z be? O A O F O E ORarrow_forwardA peptide has the sequence: Glu–His–Trp–Ser–Gly–Leu–Arg–Pro–Gly1. What would be the net charge of the molecule at pH a) 3, b) 8, and c) 11? (Use pKa values. Do not calculate the value per se, but instead estimate considering only fully protonated, or deprotonated states. Then estimate the pI for this peptide. Show full, clear and complete procedurearrow_forward
- Give the lipid number for the following fatty acid:arrow_forwardAbove or below what pH would the polypeptide become fully mobile on a cation exchange column? Explain reasoning please. Per my understanding, I believe I need to find pI and then select a pHarrow_forwardAspartic acid has a side chain bearing a carboxylic acid group; its pK, is ~4. The alpha-carboxylic and alpha-amino groups have pk, values similar to those of alanine, - 2 and ~9, respectively. Determine the net charge on an aspartic acid molecule at the following pH values (match each pH to the best choice). pH = 1 [ Choose ] pH = 2 [ Choose ] pH = 4 [ Choose ] pH = 7 [ Choose ] pH = 9 [ Choose ] pH = 13 [ Choose ] > > >arrow_forward
- Describe the amino acid illustrated here (Identify the following amino acid (at pH = 7.0): (COO-)–CH(NH3+)–CH2–CH2–CH2–CH2–(NH3+)) (at pH = 7.0). it is a polar, negatively-charged amino acid it is a non-polar, negatively-charged amino acid it is a polar, positively-charged amino acid it is a non-polar, positively-charged amino acid it is a non-polar, uncharged amino acidarrow_forwardThe 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 IVarrow_forwardThe pH of the amino acid shown below is:arrow_forward
- pI is the pH at which an amino acid exists as a zwitterion. A zwitterion has both a plus and minus charge so it is neutral overall. If the pH of a solution of tyrosine is much larger than the pI of tyrosine, which structure below represents the correct protonation state of tyrosine (tyrosine pI is 5.66; the pH of the tyrosine solution is 8.0)? NH NH H,N. HN. HO, OH но но но HO A В Darrow_forwardAn oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.arrow_forwardThe pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. 2 1.5 1 0.5 -0.5 -1 4 8 10 12 14 pH a. Which of the following triprotic amino acids is this? Histidine b. What is the isoelectric point? (Please select the appropriate range in which the isoelectric point falls) (Hint - look up the pka values in the pKa table for amino acids, which was in video one of today's lecture) 7-8 c. What form of this amino acid dominates at a pH of 8? Please select the correct form for each jonizable group. Alpha amino NH3+ Alpha carboxyl СОО- R| NH Net Chargearrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON