Consider the following protein mixture:ProteinABCDMolecularWeight (kDa)50150200350Affinity toMetal ion===Zn²+===1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select]2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select]IpH value7395[Select][Select]4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is5. The protein that will be eluted last in a gel filtration column is [Select]6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select]%Hydrophobicity204575 55

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Answered: [Select] 1. Using hydrophobic…

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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A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecularmasses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein.
Two proteins of different molecular weight (mw) are mixed and need to be separated. When eluted through a Sephadex-G50 chromatography column, what is the order of elution (first followed by second)? A. protein with mw of 40 kDa; protein with mw of 20 kDa B. both proteins will elute at the same time C. both proteins will not elute as the combined mw is larger than 50 kDa D. protein with mw of 20 kDa; protein with mw of 40 kD
You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?
calculate the volume of stock solutions required to make up the buffer solutions that will be used for protein purification. The solutions you need to prepare for purification are: i. Binding Solution A: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 5mM imidazole, 5% (v/v) glycerol ii. Wash Solution B: make up 50 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 75mM imidazole, 5% (v/v) glycerol iii. Elution Solution C: make up 10 mL 50 mM HEPES buffer (pH 7.5), 300 mM NaCl, 500 mM imidazole, 5% (v/v) glycerol please show your working . Thnk you
After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?
A mixture of proteins having molecular weights of 50 to 200 kDa can be fractionated linearly using a GFC column with an exclusion limit of at least _____.a. 25 kDab. 50 kDac. 125 kDad. 200 kDapls explain why
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?
A 20µL unknown protein was mixed with 80µL of water. Then, 10µL of this mixture was added with 10µL Bradford reagent and diluted with water to a total volume of 100µL. The absorbance at 595 nm shows 0.08 units. Solve for the protein concentration (in mg/mL) of the original unknown protein. How much protein (in mg) is in the 20uL sample? Express your answer in 3 significant figures.
detail how cation exchange chromatography works and what you would use to elute your target protein. What protein information would you need to facilitate this approach? Would you need to do any protein engineering to utilize cation exchange chromatography, justify your answer?
As an example, consider albumin, a protein made of a single polypeptide weighing 66,000 daltons (66 kDa). On the other hand, gamma globulin has quaternary structure: is made of four polypeptides, two of which weigh 23,000 daltons (23 kDa) each, and two of which weigh 53,000 daltons (53 kDa) each. When treated with reducing agent and SDS, the subunits separate and they all linearize. If albumin and gamma globulin were run through gel electrophoresis, which polypeptides would move the fastest? Which would move the slowest?
A protein sample of unknown concentration was placed in a cuvette with a path length of 1 cm and the sample was found to have an A280 value of 2.92. If the protein of interest has an extinction coefficient of 44240 M-1 cm-1 and the molecular weight of the protein is 47.411 kDa, what is the concentration of protein in mg/mL?
Using the equation for the best-fit straight line through your data, the average absorbance of your unknown samples U1 and U2, and any dilution factors (DON’T LEAVE OUT THE DILUTION FACTOR), calculate the concentration of protein in the original unknown protein sample. y = 1.6849x + 0.0414R² = 0.9904

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