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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Consider a polymeric membrane within a 6 cm diameter stirred ultrafiltration cell. The mem- brane is 30 μm thick. The membrane has pores equivalent in size to a spherical molecule with a molecular weight of 100,000, a porosity of 80%, and a tortuosity of 2.5. On the feed side of the membrane, we have a solution containing a protein at a concentration of 8 g L−1 with these properties: a = 3 nm and DAB = 6.0 × 10−7 cm2 s−1. The solution viscosity is 1 cP. The hydrody- namic pressure on the protein side of the membrane is 20 pounds per square inch (psi) higher than on the filtrate side of the membrane. Determine the convective flow rate of the solution across the membrane and the rate at which the protein crosses the membrane. The solution on the feed side of the membrane is being stirred at 900 RPM.
Standard curves You are setting up a standard curve for lysozyme. You have a stock vial containing 2 mg/ml of lysozyme and you have 2 ml in the vial. You will want to have a minimum of 1 ml of each concentration for the spectrophotometer. How would you proceed? (Saline is added to make the various concentrations). Concentration Am't stock lysozyme or am't of a previous dilution (note which) Amount saline Total volume wanted 1.00 mg/ml 0.75 mg/ml 0.50 mg/ml 0.375 mg/ml
What is the function of sodium dodecyl sulfate (SDS) in SDS-PAGE? stabilizes the gel matrix, improving resolution during electrophoresis SDS solubilizes proteins to give them uniformly negative charges, so the separation is based purely on size. SDS raises the pH of the gel, separating multiunit proteins into individual subunits. SDS solubilizes proteins to give them uniformly positive charges, so separation is based purely on pH.
What is the difference between the two salt precipitation methods: salting in and salting out? Group of answer choices Salting in relies on the isoelectric pH of the specific amino acid residue whereas salting out relies on the charge of the specific amino acid residue. Salting in relies on the charge of the specific amino acid residue whereas salting out relies on the isoelectric pH of the specific amino acid residue. Salting in decreases salt concentration thereby increasing the solubility of the protein whereas salting out increases the salt concentration to precipitate out the protein component. Salting in increases salt concentration thereby increasing the solubility of the protein whereas salting out decreases the salt concentration to precipitate out the protein component.
(a) 1 Normalized fluorescence 0.8 0.6 0.4 0.2 0 50 55 OM 0.100 M 0.200 M 0.300 M 0.500 M 1.00 M 2.00 M 60 113588 65 Temp. (°C) 70 75 80 Where is fully folded protein? • Where is fully unfolded protein? • Where is partially folded protein? • To what does SYPRO orange bind? • Why does fluorescence increase as a function of temperature? ● Define a melting temperature for a protein. • Demonstrate how an estimated melting temperature of the protein in zero molar ligand can be determined. • What is the effect of increasing the molar concentration on melting temperature for this protein? • Why is melting temperature a useful measurement to make for a protein especially if you are interested in protein aggregation?
Which of the following options shows the correct order of fastest to slowest motion of chloride ions, glycine and proteins through the separating gel? Chloride ions > Proteins > Glycine Glycine > Chloride ions > Proteins Chloride ions > Glycine > Protein Protein > Chloride ions > Glycine You are trying to separate a mixture of AMP, ADP, and ATP using ion exchange chromatography. Select appropriate supplies for your experiment. A positively charged column, deprotonated buffer, NaCl of same concentration. A positively charged column, protonated buffer, NaCl of increasing concentration. A negatively charged column, protonated buffer, NaCl of increasing concentration You cannot separate nucleotides using ion exchange chromatography.
8L.Part I
at punctures the bacterial cell wall has just been recently isolated from the F the peptide reveals the following information below: IOTE: when the sequence is nat knawn, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 °C Heptapeptide (2) Arg, Pro, Phe, Tyr, Ala, Lys 2.4-dinitrofluorobenzene DNP-Phe Lys and modified free Peptide 1 (Ala, Lys) amino acids Cleovoge with Trypsin, then chromatography Peptide 2 (Pro, Arg, Tyr) Peptide 3 (Phe, Arg) Phe Cleavage with Chymotrypsin, then chromatography Peptide 4 (Arg, Tyr) Peptide 5 (Lys, Pro, Ala, Arg) When answering the questions below, please use the ONE-LETTER CODE for the amino acid, with NO spaces and symbols between each letter. 1. What is the C-terminal residue? K 2. What is the N-terminal residue? F 3. What is the sequence of Peptide 3? GP 4. What is the sequence of Peptide 5? LPAA 5. What is the averall amino acid sequence? AL
The authors of this paper also tested another minimal media (Media C) which is exactly the same as Media B except that the pH is 7.4 instead of 7.1. Which media components would be different in Media C? For each component that is different, state if will be larger or smaller than the amount in Media B.
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Which fractions measured from your gel filtration experiment had the most and least amount of protein detected? Which fraction likely contained the most myoglobin based off molecular weight and protein presence? Which fraction likely contained the most egg albumin based off molecular weight and protein presence? Which samples measured from your ion exchange experiment had the most protein detected? Calculate the approximate pI of your proteins using the ion exchange Table 2. Ion Exchange Samples Tested by Bradford Assay Concentration BSA (μg/mL) Concentration BSA (mg/mL) Volume of Sample added to Bradford Reagent (μL) Absorbance at 595 nm Standard 1 250 0.25 50 0.32 Standard 2 125 0.125 50 0.16 Standard 3 62.5 0.0625 50 0.08 Standard 4 31.25 0.03125 50 0.04 Standard 5 15.625 0.015625 50 0.02 Blank 0.00 0.00 0.00 Table 3. Gel Filtration Fractions Tested by Bradford Assay Fraction #:…
Use correct sig figs The concentration of a purified monoclonal antibody was measured using UV280 nm. The sample was diluted (200 μL of purified antibody in 800 μL buffer) prior to analysis using a spectrophotometer. Calculate the concentration of antibody in the purified fraction if the Abs=0.95 of the diluted antibody. The molar absorptivity is known to be 191,411.6 M-1cm-1 and the molecular weight is 150 kDa. The pathlength for the cuvette is 1 cm.

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