Exercise 1Summarize the data below obtained from the protein experiments for determination of proteinconcentration in the form of a graph. Plot a graph containing a title and labels for both of theaxis. Three readings were taken for each protein concentration. Find the averages and standarddeviations for each reading and plot your graph using Microsoft EXCEL, complete with the errorbars. This graph representswill be used to measure the protein concentration in an unknown protein solution.calibration curve for a protein assay (next experiment) where thisConcentration of protein(Hg/mL)Absorbance, 595 nm1230.040.050.0320.120.110.1450.260.250.25100.490.490.51250.820.850.83501.281.241.25

The principle of the Bradford assay is based on the fact that the absorbance maximum for an acidic…

Answered: Summarize the data below obtained from…

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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You perform a Bradford assay. You obtain the absorbance values listed below from the BSA samples; your protein sample yields an absorbance of 1.3; what is the protein concentration of your sample? How did you determine that? BSA (ug/ml) Absorbance @ 595 nm. 25 0.15 50 0.30 75 0.45 100 0.60 150 0.90 200 1.25
Use correct sig figs The concentration of a purified monoclonal antibody was measured using UV280 nm. The sample was diluted (200 μL of purified antibody in 800 μL buffer) prior to analysis using a spectrophotometer. Calculate the concentration of antibody in the purified fraction if the Abs=0.95 of the diluted antibody. The molar absorptivity is known to be 191,411.6 M-1cm-1 and the molecular weight is 150 kDa. The pathlength for the cuvette is 1 cm.
Below is an EMSA showing four different reactions, A-D. In each tube there is some combination of labelled DNA probe, Protein X (the protein you are studying), and an antibody for Protein X. Identify which combination of components are found in each of the four reactions and explain how you determined that based on the molecular interactions being studied and your knowledge of gel electrophoresis. It is possible that multiple lanes have the same component(s). A B C D EMSA
Name some techniques/approaches (name, describe the major steps, how to analyze/interpret results) that can be used to satisfy the following requirements: 1. Show that substance is pure protein 2. Only one protein was extracted
A protein was purified and then analyzed on a size exclusion column. Its MW was determined to be 50,000 Dalton. The SDS-PAGE gel shows two bands, corresponding to molecular weights of 10,000 and 15,000 Dalton. Describe the native conformation of this protein in terms of the number of subunits present and their molecular weight.
(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.
Match the types of data to the example. Precise measurements Assay standard Positive control Quantitative results Negative control Qualitative results Standard curve…
Please explain how to use the global alignment algorithm: Needleman-Wunsch. Use the match 3, mismatch -3, linear gap penalty -3. Protein sequence 1: PHWG Protein sequence 2: HWEG
1a) In MALDI-TOF data, when performing peptide mass mapping search, the number of peptides and the sequence coverage decreases, but protien score increase. Explain b) As the same as part a, the peptide masses and the coverage remain the same, but the protien score increase, explain how this can happen.
You ran a gel using SDS-PAGE. Total molecular mass of your unknown protein (determined via gel filtration): 217 kDa Standard curve equation based on your protein ladder: 5205.6x^(-1.22) Number of bands in your unknown protein sample: 3 Distance each band traveled on your gel: A measured at 20 mm B measured at 62 mm C measured at 82 mm What is the subunit composition of this protein? 2 of A, 1 of B, 1 of C 1 of A, 2 of B, 1 of C 1 of A, 1 of B, 2 of C 1 of A, 1 of B, 1 of C
Among the techniques below, which method is used to study protein-protein interaction in vivo? Group of answer choices co-IP TAP Y2H All of the above
Define: simple diffusion, facilitated diffusion, primary active transport, secondary active transport and cotransport (by sure to address symport and antiport) . please explain this iin one sentense for each one please. note: I do not want more than one sentense

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