Use the table below to answer the question being asked:ProteinOvalbuminInsulinFibrinogeny-globulinCollagenHemoglobin (monomer)MyoglobinIsoelectric pH4.65.45.86.66.67.17.0Molecular weight (KDA)455.73401601151616.7A. Given the 7 proteins in the table, will they all be separated properly usingtwo-dimensional (2D) gel electrophoresis? Why or why not? Kindly justifyyour answer.B. Manually sketch the appearance after visualization of a protein mixturecontaining the 7 proteins in the table when subjected to two-dimensional(2D) gel electrophoresis.

Two dimensional (2D) polyacrylamide gel electrophoresis (2D PAGE) is a more powerful technique than…

Answered: Use the table below to answer the…

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 0.0284 M aqueous solution of lactic acid, HC3H5O3, a substance that accumulates in the blood and muscles during physical activity, is found to be 6.7% ionized. Determine the value of Ka for lactic acid.
Please answer the question below and show all your work. 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 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?
How many hemoglobin molecules are there in an average red cell? Assume that the molecular weight of the human hemoglobin tetramer is 65 kDa.
The molecular formula for glucose is C6H12O6. What would be the molecular formula for a polymer made by linking ten glucose molecules together by dehydration reactions? Group of answer choices A. C60H120O60 B. C60H102O51 C. C60H100O50 D. C60H111O51 Use the following information to answer the following questions."The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which carries a heme group. There appear to be no previous studies that report the in-vitro folding and assembly of Hb from highly unfolded α and β globin in a 'one-pot' reaction. One difficulty that has to be overcome for studies of this kind is the tendency of Hb to aggregate during refolding. This work demonstrates that denaturation of Hb in 40% acetonitrile at pH 10.0 is reversible." (J Am Soc Mass Spectrum 2007, 18, 8-16)In sickle-cell disease, as a result of a single amino acid change, the mutant hemoglobin tetramers associate with each other and assemble into large fibers.…
Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 75,000 5.0 No 2 12,500 4.8 No 3 73,000 9.8 Yes a. What type of chromatography separates proteins based on their size? b. What type of chromatography separates proteins based on their charge? c. Could gel filtration chromatography be used to separate a mixture containing Protein 2 and 3? Clearly explain why or why not. If gel filtration chromatography can be used to separate Protein 2 from Protein 3, which protein would elute first (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins (Protein 2 and Protein 3) be monitored at 280nm and 400nm (clearly explain)? d. Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by…
Give only typing answer with explanation and conclusion You want to make 94 µL of the diluted Cell-Free extract for estimation of total protein. To do this, how much water will you add to the correct volume of the undiluted cell-free extract? Note: Cell-free extracts will need to be diluted 1:25 in water.
Creatinine, C4H7N3O, is a by-product of muscle metabolism, and creatinine levels in the body are known to be a fairly reliable indicator of kidney function. The normal level of creatinine in the blood for adults is approximately 1.0 mg per deciliter (dL) of blood. If the density of blood is 1.025 g/mL, calculate the molarity of a normal creatinine level in a 10.0 mL blood sample.
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
Avidin exists as a protein complex of around 68 kDa. Research to determine the types of interactions that hold the avidin complex together. Based on your research, which molecular weight would you expect for avidin when treated with beta-mercaptoethanol and run through an SDS-PAGE gel? Question options: 34 kDa 19 kDa 68 kDa 11 kDa
Using the data in the table below, calculate the average molar mass of an amino acid residue in each of the proteins in the table (excluding cytochrome c, myoglobin, and hemoglobin). Next, calculate the mean of the mean molar mass considering all proteins (excluding cytochrome c, myoglobin and hemoglobin)
Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 25,000 4.5 Yes 2 77,500 10.8 No 3 75,000 4.9 No a) Could gel filtration chromatography be used to separate a mixture containing Protein 1 and 2? Clearly explain why or why not. If it can be used, which protein would elute last (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins 1 and 2 be monitored at 280nm and 400nm (clearly explain)? b) Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by gel filtration? Why? c) Which 2 proteins listed in the table above could be separated by gel filtration chromatography but NOT by ion exchange chromatography? Why?
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?

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