BIOCHEMISTRY
9th Edition
ISBN: 2818440090622
Author: BERG
Publisher: MAC HIGHER
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Chapter 3, Problem 21P
Interpretation Introduction
Interpretation:
The description of the structure of the molecule resulted from the 6M urea and 10 mM ß-mercaptoethanol should be determined.
Concept introduction:
Gel filtration chromatography is a type of chromatography. It is useful in the separation of proteins based on size. It is also known as the gel permeation or molecular exclusion chromatography.
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A protein was purified to homogeneity. Determination of the mass by gel-filtration chromatography yields 60 kDa . Chromatography in the presence of 6 M urea yields a 30-kDa species. When the chromatography is repeated in the presence of 6 M urea and 10 mM β - mercaptoethanol , a single molecular species of 15 kDa results. Describe the structure of the molecule.
A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the native protein has a molecular weight of 300,000. Chromatography of the protein in the presence of 6 M guanidine hydrochloride (a denaturant) yields a single peak corresponding to a molecular weight of 50,000. Chromatography of the protein in the presence of 6 M guanidine hydrochloride and 10 mM beta-mercaptoethanol (a disulfide bond reductant) yields peaks corresponding to molecular weights of 30,000 and 20,000. What does this data tell you about the structure of this protein? (Be thorough in your answer!)
The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).
Chapter 3 Solutions
BIOCHEMISTRY
Ch. 3 - Prob. 1PCh. 3 - Prob. 2PCh. 3 - Prob. 3PCh. 3 - Prob. 4PCh. 3 - Prob. 5PCh. 3 - Prob. 6PCh. 3 - Prob. 7PCh. 3 - Prob. 8PCh. 3 - Prob. 9PCh. 3 - Prob. 10P
Ch. 3 - Prob. 11PCh. 3 - Prob. 12PCh. 3 - Prob. 13PCh. 3 - Prob. 14PCh. 3 - Prob. 15PCh. 3 - Prob. 16PCh. 3 - Prob. 17PCh. 3 - Prob. 18PCh. 3 - Prob. 19PCh. 3 - Prob. 20PCh. 3 - Prob. 21PCh. 3 - Prob. 22PCh. 3 - Prob. 23PCh. 3 - Prob. 24PCh. 3 - Prob. 25PCh. 3 - Prob. 26PCh. 3 - Prob. 27PCh. 3 - Prob. 28PCh. 3 - Prob. 29PCh. 3 - Prob. 30PCh. 3 - Prob. 31P
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- A protein of unknown structure has been purified. Size-exclusion chromatography reveals that the native protein has a MW of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of MW 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM B-mercaptoethanol yields peaks for proteins of MW 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.arrow_forwardPlease don't provide handwriting solutionarrow_forwardCan you please show me how to work this out and which fraction in the picture provided is correct? Thank you!!arrow_forward
- A protein was purified to homogeneity. Determination of the mass by gel filtration chromatography yields 60 kd. Chromatography in the presence of the denaturing agent, 6 M urea, yields a 30 kd species. When the chromatography is repeated in the presence of 6 M urea and DTT, a single molecular species of 15 kd results. Describe what these experiments tell you about the structure of the proteins.arrow_forwardGiven: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?arrow_forwardThe following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bondsarrow_forward
- Predict the number of bands and apparent mol. wt. of the following proteins on SDS gels. 1. A trimeric protein containing three chains, each with a molecular weight of 60,000 Da (60 kDa).arrow_forwardWh are doing this procedures can you explain? (ex. heating or adding chemicals etc.) 1) Purification of Vitelline from Egg Yolk-Experimental ProcedureMeasure the volume of 3 egg yolks and mix by adding an equal volume of NaCl solution.Extract the mixture with 3-fold volumes of ether and separate the aqueous phase.Do the same procedure 3 times.Mix the sample with water and rinse.It is expected for the protein to collapse.Some more water is added in order to check whether the collapse occurs completely.The sample is centrifuged and the precipitate is dried. 2) Purification of Plasma Albumin and Fibrinogen-Experimental ProcedureAdd ammonium sulfate to 10 ml plasma up to 25% saturation.Separate the collapsed fibrinogen by centrifuge.Increase the saturation level to 33% by adding (NH4) 2SO4.Separate the globulin by centrifugation.Separate prodoglobulins by increasing the saturation level to 46%.Increase the saturation level up to 64% to precipitate albumin.Separate the albumin by centrifuge…arrow_forwardHelp me pleasearrow_forward
- On an SDS-gel, If the distance traveled by the bromophenol blue dye is 7 cm, and the distance traveled by the protein band is 2.8 cm, the mobility of the protein is 40 4 40% 0.4arrow_forwardIf the absorbance at540nm of a biuret and protein solution containing 0.25mg/ml of protein .24 the absorbance of a biuret and protein and dna solution containing.25mg/ml of protein and 0.5mg/ml dna should be note the total volume is the same in both solutions 0.24 0.72 0.48 not enough inforarrow_forwardDo not give handwriting solution.arrow_forward
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