The following table shows the distance moved in an SDS-polyacrylamide gel by a series of markerproteins of known relative molecular weight.a. If the tracking dye had moved a distance of 90.0 mm, calculate linear regression parameters such aslinearity coefficient (r), the slope (m), and the y-intercept (b).ProteinMW (DaDistance moved (mm)Transferrin78 0006.0Bovine serum albumin66 00012.5Ovalbumin45 00032.054.0TrypsinogenMyoglobinLysozymeCytochrome c24 00017 80069.014 30079.012 40086.5Proliferating cell nuclear antigen (PCNA) acts as a homotrimer of three identical subunits and helpsincrease the processivity of leading strand synthesis during DNA replication. It has a molecular weightof 36.0 kDa. Under the reducing conditions of the sample buffer, the disulfide bridges linking thesubunits are reduced and thus the monomer chains are seen on the gel.b. Calculate the Rf of the single band of PCNA when subjected to SDS-PAGE.c. Predict the distance (in mm) that will be traveled by the band. Report your answer in one (1) decimalplace.

The X-axis of the SDS PAGE Standard Plot is Relative Migration (also called Rf) , while the Y-axis…

Answered: The following table shows the distance…

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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1) If there were two distantly protein, the best BLOSUM & PAM matrix is: ① BLOSUM 45 and PAM 250 ② BLOSUM 45 and PAM 1 ③ BLOSUM 80 and PAM 250 ④ BLOSUM 80 and PAM 1 Give typing answer with explanation and conclusion
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).
Fluorescence confocal microscopy (FCM) - STK38 monoclonal antibody (M01), clone 2G8- 1F3. a. b. 200 μm What is the basic principle of image formation using this microscopy technique? What can be observed and concluded from the image of the specimen?
A 10 μL-aliquot of a resuspended genomic DNA stock solution was obtained and further diluted by adding 990 μL TE buffer. The A260 of the resulting solution was 0.316. Determine its concentration in µg/µL.
Western blotting is a routine technique in protein analysis that provides qualitative and semi- quantitative data. In this work, protein separation is first carried out using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). (i) Explain the principle of SDS-PAGE in protein separation. After the electrophoretic separation, the proteins are transferred to a nitrocellulose membrane prior to staining with antibodies specific for the protein understudy. Describe in detail how the primary and secondary antibodies could aid in the protein detection process. (ii)
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
(b) Both laboratories used 10 micrograms of protein each in their kinetic assays. Protein concentrations weredetermined by the Bradford protein assay. Assay conditions employed in the two labs (pH, temperature,etc.) were also identical. What would be the most plausible cause for the discrepancy in the Vmax valuesfor the compound I? Explain.Recall that the Bradford assay measures total protein amounts in sample solution based on complexformation between a dye and proteins. Also, the assay solution used in both labs does not contain anyinhibitors.
If 1ml of an unknown sample of protein is diluted to 10ml, and a 0.5ml portion of the diluted sample is found to contain 50ug of protein when assayed for protein using the lowry method. If you mix two unknown samples and repeat the lowry assay, is the absorbance equivalent to the sum of the two individual unknown samples that is used?
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
Hidden Markov Model (HMM) Construct the HMM for the following sequences 2) G C A A A A G A A T G C A A G A The matches are considered for the columns [1, 2,4,5, and 7]
List and Describe the algorithm of BLOSUM substitution matrix computation.
Estimate the viscosith of 1.0 vol % agarose gel solution if it took 58 minutes for 1500 base pairs long DNA molecule to migrate 11cm during gel electrophoresis under 110V. Assume appropriate numerical values for the missing parameters such as the charge and diameter of DNA molecules.

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