2. Mixtures of amino acids can be analyzed by first separating the mixture into its componentsthrough ion-exchange chromatography. Amino acids placed on a cation-exchange resincontaining sulfonate (-SO₁) groups flow down the column at different rates because oftwo factors that influence their movement: (1) ionic attraction between the sulfonateresidues on the column and positively charged functional groups on the amino acids, and(2) hydrophobic interactions between amino acid side chains and the strongly hydrophobicbackbone of the polystyrene resin. For each pair of amino acids listed, determine whichwill be eluted first from the cation-exchange column by a pH 7.0 buffer. (a) Asp and Ly,(b) Arg and Met, (c) Glu and Val, (d) Gly and Leu, (e) Ser and Ala

At a pH of 7, the side chain of some of the amino acids will be positively charged, some will be…

Answered: Mixtures of amino acids can be analyzed…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. Net Charge 0 2 4 Alpha amino [Select] 6 R [Select] pH a. Which of the following triprotic amino acids is this? Alpha carboxyl [Select] 8 10 12 [ Select] 14 1 0.5 0 -0.5 -1 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) [Select] -1.5 c. What form of this amino acid dominates at a pH of 14? Please select the correct form for each ionizable group. -2
Angiotensin Converting Enzyme (ACE) is the target of ACE inhibitors such as captopril that are used therapeutically to control blood pressure. The enzyme ACE converts angiotensin I to angiotensin II. Angiotensin II is an octapeptide with the sequence Asp-Arg-Val-Tyr-Ile-His-Pro-Phe. What will its net charge be at pH 7? A) -2 B) -1 O C) O D) +1 E) +2
Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5). Part C: Justify your answer with calculations of partial charges on these amino acid side chains at pH=7.9.(Hint: Consider lessons from Coulomb's law, and the Henderson-Hasselbalch equation.)
Do the titrated amino acids appear to be acidic, basic, or neutral amino acids? Explain your conclusion with reference to the data and to theory.
Identify the following types of biomolecules and label and identify all of the functional groups.
What is the predominant ionic form of ribose-5-phosphate at physiological pH? Would ribose-5-phosphate be a good biological buffer for cells?
Disulfide bonds help to stabilize the three-dimensional structure of proteins. What amino acids are involved in the formation of disulfide bonds? Does the formation of a disulfide bond increase or decrease entropy (ΔS)?
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
a. what general category would you place this molecule in of the four categories of biomolecules? b. List 5 functional groups you see in this molecule?
Refer to the following titration curve below: 13 12 11 10 7 5 4 3 2 8 10 12 14 16 18 20 22 24 26 28 30 Volume of Titrant / mL Unknown Acid 0.10 mol/L - titrant = NaOH 0.1 mol/L How many buffering regions are present in the titration curve of the amino acid?
After treatment with peroxyformic acid, the peptide hormone vasopressin is partially hydrolyzed. The following fragments are recovered. Propose a primary structure for vasopressin. Phe-Gin-Asn Pro-Arg-Gly NH2 Cys-Tyr-Phe Asn-Cys-Pro-Arg Tyr-Phe-Gin-Asn
1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?

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