The following data is protein melting point (Tm) characterization data obtained by the ZetasizerNano System (Dynamic Light Scattering method, DLS)². The melting point for the series of proteinsare measured in PBS (phosphate buffered saline). Which protein is structurally the most stableform in PBS? State your reasoning in full sentence.Z average in DLS: The dynamic size of particle.*100ProteinT.(°C)386571646890Bovine HemoglobinBovine Serum AlbuminOvalbuminHuman InsulinHen Egg Lysozyme80706050403020103035404550556065707580Temperature (°C)Z Average Diameter (nm)

Proteins are biopolymers synthesized in the cells through translation. The proteins produced through…

Answered: The following data is protein melting…

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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6 Concanavalin (ConA) is a 25.5KDa protein with pI of 4.7 and optical absorbance (A 0.1% 289) of 1.14. calculate the concentration of an aqueous solution of pure BSA protein with an absorbance of 0.66 at 280nm. give your answer in units of mg/ml ?
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…
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 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.
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?
You are given a protein solution with a concentration of 0.15 mg/ml. Suppose that we want to prepare a solution containing 100 μg of the protein at a concentration of 1 mg/ml. To achieve this, we will first dry down enough protein solution to obtain 100 μg of proteins. How much solution do we need for drying down? How much volume of H2O do we need to add to the dried protein to obtain the desired concentration?
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
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?
What is the melting temperature and G/C content of the following primers? a.) 5’ GAAATAATTTTGTTTAACTTTAAG 3’ b.) 5’ GTAACTCAGCTTTCAGGTCG 3’
A mixture of proteins contains four different polypeptides, all in ~equal concentration, in solution with the following properties: Protein Molecular Mass (kDa) Isoelectric point A 45 4.5 B 77 6.0 C 28 4.1 D 14 10.7 A fraction of the protein solution is applied to a strong cation exchange column using a buffer at pH 8.0 with increasing [NaCl] from 0.05 M – 1.0 M. The chromatogram is shown below: 1. Based on the data presented, which of the following statements is true: Peak #1 is protein D Peak #4 is protein C Peak #3 is protein A Peak #4 is protein D Peak #2 is protein B 2. Since you know that the proteins are all present in approximately equal concentrations, the different relative peak areas tell you that: There are more neutral amino acids in protein #4…
You assay 0.5 ml of 1/2000 diluted egg white for protein, as described in the practical schedule, and the spectrophotometer reading at 595 nm is 0.6. Using the attached calibration curve(click to enlarge), calculate the concentration of protein in undiluted egg white. Give your answer in mg/ml.

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