After calculating the extinction coefficient for lysozyme above, you convert it intoml mg cm1 units. (You need not do the calculation, just suppose you did).To calculate the protein concentration in your column fractions (W1-3, E1-2), wouldyour calculated extinction coefficient be a better choice than 1.5 mL mg 1 cm1 valuelisted in the theory section of your pre-lab? Why or why not?(Choose the best response)Yes, because we expect all of the column fractions to be mainly lysozyme.No, because most, if not all, the column fractions are mixtures of 2 or moreproteins.Trick question, we should use the values calculated by EXPASY for lysozyme.Yes, because my calculated value is more accurate than values from theliterature.ONo, because lysozyme is still stuck to the column and shouldnot be in any of ourcolumn fractions.

Lysozyme is a low molecular weight enzyme (~14kDa), it hydrolyzed the beta-1,4 linkage between…

Answered: After calculating the extinction…

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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Similar questions

This is a visible spectra between 390-590 nm obtained during the protein separation process of haemoglobin and cytochrome c using CM Sephadex chromatography. I'd like the results shown on the image interpreted. Look for characteristic peaks or patterns that correspond to the absorption properties of these proteins in the visible range.
Can Hydrophobic Interaction Bead Chromatography be used to isolate Protein X from muscle tissue if Protein X contains many hydrophobic regions? Explain the process of how to isolate Protein X from muscle tissue.
Determine the concentration of monocytogenes enumerated from the apple slice based on the information below. You must draw your serial dilution and show your mathematical calculation to receive full credit. The apple slice (12 g) was first mixed with 108 ml of sterile 0.1% peptone water. After, 1 ml was added to tube containing 9 ml of sterile 0.1% peptone water. Process was repeated with two additional tubes. 1 ml was pipetted from tubes 2 and 3 onto MOX media. Plates were incubated at 37 for 48 hours. The pictures below show the plates from tube 2 (left) and tube 3 (right).
If the enzyme maltase has a Vo of 0.25 mM per minute when [S] = 0.10 mM, and a Vo of 0.40 mM perminute when [S] = 0.40 mM, what is its y-intercept on a Lineweaver-Burk plot?A. 0.10 minutes per mMB. 0.20 minutes per mMC. 0.50 minutes per mMD. 1.0 minutes per mME. 2.0 minutes per mM
Make a table with a scale of absorbance and the concentration of protein in Chromatin sample from the following data for excel graph Absorbance=660nm following data are of tubes with concern A =0 B=0.036 C=0.011 D=0.001 E=0.027 F=0.020 G=0.032 H1=0.176 H2=0.183 I1=0.150 I2=0.171 also plot the graph??
You perform electrophoresis of 3 proteins, Hemoglobin (pl: 6.8), DNA Polymerase (pl: 5.2) and Porcine pepsin (pl: 1.0) in a Tris-Glycine buffer (pH 5.2). (pl = Isoelectric point). Select which of the following is true. O All proteins will migrate at the same rate O All proteins will migrate at the same direction Porcine pepsin will migrate toward the electrode Porcine pepsin will not migrate and stay in the well
In RP HPLC, one of the most common separation methods used to measure purity, strength, dosage, etc, a protein would be put into 0.1% (1000 ppm) TFA (Trifluoroacetic acid), what do you suppose this does to the protein in many cases? (Pick the BEST answer). somewhat denaturing to very denaturing oxidizes cysteine ionizes acid and base groups
When protein X is subjected to dimethylsuberimidate and SDS electrophoresis a 50 kDa band is seen; when the protein X is subjected to SDS electrophoresis without DMS, two bands of 20 kDa and 10 kDa are seen. How many different oligomeric structures of the native protein X are possible, being consistent with these observed results? one two three none of the above which is the answrr? and explain
If the enzyme maltase has a Vo of 0.25 mM per minute when [S] = 0.10 mM, and a Vo of 0.40 mM perminute when [S] = 0.40 mM, what is its y-intercept on a Lineweaver-Burk plot?A. 0.10 minutes per mMB. 0.20 minutes per mMC. 0.50 minutes per mMD. 1.0 minutes per mME. 2.0 minutes per mM
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?
Consider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal 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 is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. 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] % Hydrophobicity 20 45 75 55
Xylose racemase is a bacterial enzyme that converts the sugar D-xylose to L-xylose, which is needed in small amounts for the bacterial cell wall. The active site of xylose racemase includes a Y residue with a pKa = 7.2. The altered pKa of this residue, compared to its pKa in bulk water, is due largely to the presence of a nearby charged amino acid residue in the active site. Which is a likely explanation for the shift in the Y residue pka? The negative charge in a nearby E residue could stabilize a deprotonated Y residue. The negative charge in a nearby D residue could destabilize a protonated Y residue. The positive charge in a nearby K residue could stabilize a deprotonated Y residue. The positive charge in a nearby R residue could destabilize a deprotonated Y residue.

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