2. You have 15mL of a 0.3M solution of His-Lys-Leu-Asp adjusted to pH=9. Youtitrate your solution with 10mL of 0.2M HCl. Relevant pka values are2.1,3.8,6.0,9.8 and 10.5.A) Draw the structure of the tetrapeptide that predominates in solutionbeforeyouaddanyHCl.B) Calculate the new pH value of the solution after the addition of HCI.C) You digest this tetrapeptide with trypsin at pH=( and apply the products toan anion exchange column. Write the amino acid sequence of the productsthat are produced. If you gradually add HCl to the column, in what order willthese products elute, if at all?

Given, Original solution: 15 mL(0.015 L) of 0.3M ; pH= 9 Titrant: 10 mL(0.01 L) of 0.2M HCl= pH=…

Answered: You have 15mL of a 0.3M solution of…

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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1.The specific rotation of a sample of mandelic acid [PhCH(OH)CO2H] is -9.48° and of pure S-(-)- mandelic acid is -158°. Calculate the (1) % optical purity, (2) ee, (3) % composition and (4) draw a clear stereo-structure for S-(-)-mandelic acid. 2. Explain each of the following concepts: a)positional isomerism b) Newman projection formula c) Chemoselectivity 3. use the molecular formula C4H8O2 to illustrate the following isomers: a) (+)-gauche and antiperiplanar b) chain isomer c) Enantiomer d) Cis-and Trans cycloalkanes
6 (a) A decapeptide has the following amino acid composition: Ala2 , Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine. From the experimental data, deduce the primary structure of the decapeptide. (b) Suggest a scheme you will follow to synthesize the dipeptide Ala-Gly
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?
4 How do I convert from DPM to picomoles per milligram of protein (pmol/mg)? I have the specific activity as [3H]-spiperone is 25530 DPM/pmol. is there an equation?
2) You are studying the tripeptide Lys-Val-Thr. a) Draw the full structure of the tripeptide Lys-Val-Thr at pH 7 and label each of the following in your drawing:i) atoms that are co-planar in one pep de bond ii) one φ (phi) and one ψ (psi) angle b) Could you use the absorbance at 280 nm to determine the concentra on of this tripep de? Briefly explain your answer
6 Concanavalin (ConA) is a 25.5KDa protein with pI of 4.7 and optical absorbance (A 0.1% 289) of 1.14. calculate the concentration of an aqueous solution of pure BSA protein with an absorbance of 0.66 at 280nm. give your answer in units of mg/ml ?
Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.5; Pk2 = 10.8; PkR = 8.5 His: Pk1 = 1.6; Pk2 = 9.0; PkR = 7.0 Lys: Pk1 = 2.2; Pk2 = 8.5; PkR = 9.8 a.draw the protonic equilibria for the tripeptide. b.what is the IpH? c.What is the dominant structure at pH 3.0? d.What is the first buffering region of the tripeptide?
Ferritin is treated with SDS or SDS and b-mercaptoethanol and subjected to polyacrylamide gel electrophoresis. Only when very large amounts of bisacrylamide are added do you see two separate bands on the gel at relative migrations of 4.0245 and 3.9375 and the results are the same with and without b-mercaptoethanol. You decide to call these the light and heavy chains of ferritin. What are the actual sizes of the light and heavy chains of ferritin based on the SDS-PAGE data? What types of interactions hold these proteins together in the structure of ferritin?
1. If Ser 80 was replaced with Arg what kind is the change in the bond type between these two molecules? Will this change be more or less stable. Explain
One liter of a 0.1 M Tris buffer (pKa of Tris = 8.3, see Table 2.4) is prepared and adjusted to a pH of 2.0. A) What are the concentrations of the conjugate base and weak acid at this pH?Answer with 2 significant digits. I have solved for [HA] = 0.10 Can you please help solve for [A-] = ?
1. a. draw the L- & R- stereoisomer of the amino acid T using a fischer projection or a newman projection. b. draw the tripeptide LEM in the protonation state you would expect at physiological pH. show the position of phi and psi angles on the E residue
1. a. Explain why the melting point of palmitic acid (16 carbons, no double bonds) is slightly lower thanthat of stearic acid (18 carbons, no double bonds). Explain why the melting point of oleic acid (18carbons, one double bond) is lower than that of stearic acid b. A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.

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