. Suppose you have two genetic variants of a large protein that differ only inthat one contains a histidine (side chain pk, = 6.0) when the other has avaline (uncharged side chain).(a) Which would be better for separation: gel electrophoresis or isoelectricfocusing? Why?(b) What pH would you choose for the separation?

The separation techniques used in biochemistry: Gel electrophoresis: The basic separation techniques…

Answered: . Suppose you have two genetic variants…

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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2 / 9 100% +| 1. Explain why only small areas of the Ramachandran plot (below) are occupied (shaded grey) and what the two dark grey shaded areas represent in terms of a protein structure. +180 120 60 -60 -120 -180 -180 -120 -60 60 120 +180
→x D. Two physical 5. A protein unfolds according to the scheme N properties (property 1 and 2) are measured at three points in the unfolding reaction where the true values of fp are 0.2, 0.5 and 0.8. The corresponding values of K = fx/ fp are 1.0, 0.4 and 0.125. For property 1, d₁ = 0.1; for property 2, d₁ = 0.2. (a) Write an equation that can be used to calculate fapp. (b) Calculate fapp using d₁ = 0.1 (property 1) and fapp using d₁ = 0.2 (property 2). (c) The error in measurement of each physical property is 5 %. Can you detect the presence of the intermediate by measuring the physical properties? Explain your answer
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You are working as a Research Scientist I at Albany Molecular Research. For one of your bacterial growth media, you need to prepare 1.4 liters of a 35mM sucrose solution. What do you need to do? MW of sucrose is 342 g/mol Oa. dissolve 168 g of sucrose in ~ 1 liter and fill total volume to 1.4 liters O b. dissolve 8.55 g of sucrose in ~ 1 liter and fill total volume to 1.4 liters c. dissolve 16.8 g of sucrose in ~ 1 liter and fill total volume to 1.4 liters N d. dissolve 14.1 g of sucrose in~ 1 liter and fill total volume to 1.4 liters O e. dissolve 16.8 g of sucrose in 1.4 liters
The concentration of protein in a solution can be determined via UV spectroscopy and colorimetry* techniques. Explain further on the statement, give examples of the techniques (please provide three examples for the colorimetry), general principles/mechanism, and general procedures of the techniques. You may use a Table to present the answer. If you need to choose a technique to measure your protein sample, what would be your choice? Justify your answer.
You're on duty at a prominent Metro laboratory. You mixed up a sample for protein analysis of the samples needed for forensic examination that contains pure DNA while waiting for your closest friend. You decided to use the knowledge you gained in Biochemistry to run the combined samples through a spectrophotometer to eliminate contaminated protein. Determine which of the samples should be extracted and separated for protein analysis based on the following data. Show all of your solutions. A230 A260 A280 Buffer 0.051 0.091 0.065 Sample A 1.27 4.54 2.01 Sample B 1.32 3.92 2.11 Sample C 1.95 3.88 2.04 Sample D 1.44 4.21 2.32
ch2
which in is the best method for separating proteins A and B that have the properties below: Protein A: a tetramer of identical 80kDa subunits with a pl of 6.4 Protein B: a monomeric protein with a MW of 80kDa and a pl of 9.2 A.) Anion exchange chromatography at pH 11 B.) Gel exclusion chromatography C.) Cation exchange chromatography at pH 4 D. Cation exchange chromatography at pH 11 E.) SDS-PAGE
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His-Phe-Arg–Trp–Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala | (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…
You ran a gel using SDS-PAGE. Total molecular mass of your unknown protein (determined via gel filtration): 217 kDa Standard curve equation based on your protein ladder: 5205.6x^(-1.22) Number of bands in your unknown protein sample: 3 Distance each band traveled on your gel: A measured at 20 mm B measured at 62 mm C measured at 82 mm What is the subunit composition of this protein? 2 of A, 1 of B, 1 of C 1 of A, 2 of B, 1 of C 1 of A, 1 of B, 2 of C 1 of A, 1 of B, 1 of C
Suppose you have a solution of a protein, which contains a specific Tyr residue that has an actual (measured) pKa of 8.8. The protein binds a ligand by several noncovalent interactions, one of which is a hydrogen bond in which the Tyr phenolic hydroxyl group must serve as a hydrogen bond donor. Calculate the percentage of the protein molecules in which that tyrosyl residue's phenolic hydroxyl group could serve as a hydrogen bond donor at pH 8.5
What features of protein structure allow separation by Size exclusion ("gel-filtration") chromatography: (explain your answer)

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