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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A series of bovine serum albumin (BSA) was prepared and 1 mL of each solution was subjected to a Bradford assay. The increase in absorbance at 595 nm relative to the concentration of protein was plotted as shown below. Save 1.0- 0.8- 0.6- 0.4- 0.2- 0.04 0.0 0.5 1.0 2.0 2.5 1.5 BSA concentration (mg/mL) a) Using the graph, calculate the original concentration of protein present in a mixture of haemoglobin and methylene blue (diluted 1:50), which gave an absorbance of 0.20 at a wavelength of 595 nm using the Bradford assay. Show all workings. Absorbance (O.D.)
A sample of a protein is analyzed by CE using a neutral-coated capillary with a total length of 25.0 cm and a distance to the detector of 22.0 cm. Using an applied voltage of 20.0 kV, the protein was detected at a migration time of 16.2 min. The diffusion coefficient for the protein is 2.4 x 10-7 cm?/s. (a) Calculate the apparent electrophoretic mobility of the protein. (b) Calculate the expected number of theoretical plates for the analysis.
1.0.1 mL of a protein solution of concentration of 11 mg/mL was diluted to a total volume of 4.0 mL with water (i.e. 0.1 mL of the solution was added to 3.9 mL of water). 2 mL of this solution was then mixed with 18 mL of water. What is the concentration of the diluted protein solution? Space to show your workings:
You run 5 standard proteins listed below on a size-exclusion (gel filtration) column with limit of 200,000Da. Please draw a chromatogram on a separate page with each peak and both axes labeled. Protein B-Amylase Alcohol dehydrogenase Bovine albumin Carbonic anhydrase Cytochome A280 MW 223,800 0.5 82,000 0.6 66,463 0.45 30,000 0.43 12,000 0.8
the 2 answers for both questions are right are right i just need the steps, i gave you 2 questions so you can double check your that the steps are right
I am not understanding why TA of alcohol precipitation is used as TA of purified protein. I provided 2 photos, 1 with the questions and the correct answer, and the other photo is a screenshot of the explanation.
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
PLEASE have the following and help D:. What i need for the chosen of 2/3 choices. 2) Illustrate detailed chemical scheme for how you will functionalize your biomolecule to the surface of the sensor (e.g. if you wanted to functionalize a protein to a gold SPR chip, you should could show the assembly of an amine-terminated SAM, followed by carbodiimide coupling of. the protein). These schemes should be drawn using a chemical illustration software package (ChemDraw / ChemSketch).Your chemical schemes should be as detailed as necessary to accurately depict the chemical design of your system, DO NOT INCLUDE a step-wise mechanism, it is not necessary. You should include at least one literature reference to support your conjugation strategy.3) Include an illustration of the functional sensor, and describe whether the sensor is label-free or not, what signal is observed, and how you would detect the interaction (i.e. if a labeled antibody is required, you should describe what label would…
Calculate the amount of protein (in mg) in Sample 1 if the measurement at A280 = 0.636, taking into account the dilution factor as per question 6 (100ul) and the total volume of extract as per question 4 (140ml). Give your answer as a number with no decimal places.
Protein Solubility 3.5 5.5 5 5 0.068 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.130 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 15 PH 7.5 1.5 4.5 5 0.027 3 0.042 Protein Solubility Versus pH 6.5 6 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 7.5 7.5 50 0.032 0.053 8.5 50 0.054 0.100 21.429% 9 Please provide a brief discussion and explanation of the results. (using isoelectric point and net charge to explain)
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?
What is the chemistry principle behind when (treatment: heavy cream, evaporated milk, and NFDM) is subjected to different types of temperature such as room tempt and chilled. Why does beating time, stability (%drain) and volume foam (specific gravity) is important? see the data below Treatment (Heavy Cream) Beating Time (min) Stability (%drain) Volume of Foam (Specific Gravity) (Room Temperature) 20 No drain 0.94 Heavy Cream (chilled) 20 No drain 0.76 Heavy Cream with sugar and vanilla 20 No drain 0.88 Heavy Cream (over-whipped) 25 No drain 0.83 Treatment (Evaporated Milk) Beating Time (min) Stability (%drain) Volume of Foam (Specific Gravity) (Room Temperature) 8 No drain 0.33 Evaporated milk (chilled) 11 No drain 0.86 Evaporated milk with lemon and sugar 12 No drain 0.87 Evaporated milk with gelatine and water 10 4.57% 0.50 Treatment (NFDM) Beating Time (min) Stability…

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