1107L-QAP-PerezB

This graph represents a standard curve from a BCA assay for protein concentration. If your BCA reaction with your unknown protein has an absorbance of 0.2, approximately what concentration of protein is in your unknown sample? Absorbance (562nm) 0.5 0.45 3 0.35 0.3. 0.25 0.15. 0.1- 0.05 ~0.1 μg/ml ~4.5 μg/ul less that 0.005 | 0.2 μg/μ. [Protein (BSA)) (pg/ml)

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).

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

Protein concentration standards 0.6 0.5 0.4 0.3 0.2 0.1 0.5 1.5 2.5 Albumin concentration (mg/mL) A standard curve of known concentrations of protein were reacted with the Biuret reagent. A linear curve fit is presented above. • Use the graph to estimate the concentration of an unknown sample with an A550 value of 0.416 (A rough estimate is fine. You do not need a calculator for this problem) • Use the graph to estimate the concentration of an unknown sample with an A550 value of 0.233 • Which instrument did we use to measure the intensity of the color of proteins that reacted with Biuret reagent?

1- Describe any errors in your technique. How could you improve upon your technique in order to get a better and more accurate standard curve graph? 2-Estimate (from your data) the [Protein] of your unknown (0.103) based on comparing to the standards. Include the correct unit. This estimate should be an integer (no decimals).

A protein gives a single band on SDS gel electrophoresis, as shown inlanes 1 and 2 below. There is little, if any, effect from adding β-mercaptoethanol (BME) to the sample; if anything, the protein runs a little bitslower. When treated with the proteolytic enzyme thrombin and electrophoresis in the absence of BME, the protein migrates a bitmore rapidly (lane 3). But if BME is present, two much more rapidlymigrating bands are found (lane 4). Explain these results in terms of amodel for the protein.

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y biochemical calculation w linear regression parameters. please write complete values and answer all

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Wh are doing this procedures can you explain? (ex. heating or adding chemicals etc.) 1) Purification of Vitelline from Egg Yolk-Experimental ProcedureMeasure the volume of 3 egg yolks and mix by adding an equal volume of NaCl solution.Extract the mixture with 3-fold volumes of ether and separate the aqueous phase.Do the same procedure 3 times.Mix the sample with water and rinse.It is expected for the protein to collapse.Some more water is added in order to check whether the collapse occurs completely.The sample is centrifuged and the precipitate is dried. 2) Purification of Plasma Albumin and Fibrinogen-Experimental ProcedureAdd ammonium sulfate to 10 ml plasma up to 25% saturation.Separate the collapsed fibrinogen by centrifuge.Increase the saturation level to 33% by adding (NH4) 2SO4.Separate the globulin by centrifugation.Separate prodoglobulins by increasing the saturation level to 46%.Increase the saturation level up to 64% to precipitate albumin.Separate the albumin by centrifuge…

SDS-PAGE gels are useful in determining the molecular weights of proteins; however, the molecular weights of are usually not reliable. protei

Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.

Simple problem-solving: Imagine you did a Bradford assay, and measured the absorbance of a set of protein standards and two unknowns. You repeated each measurement three times, and got the following readings in the table below. Concentration (micrograms/ml) A595 - trial 1 A595- trial 2 A595- trial 2 average A595 A595 of sample minus A595 of blank 0 1.501 1.446 1.447 1.465 0 2 1.624 1.558 1.559 1.580 0.115 5 1.731 1.749 1.712 1.731 0.266 10 1.901 1.838 1.892 1.877 0.412 15 2.161 2.108 2.228 2.166 0.701 18 2.231 2.277 2.319 2.276 0.811             unknown 1 - D1 1.717 1.713 1.644 1.691 0.226 unknown 2 - D1 1.668 1.649 1.656 1.658 0.193 concentration of unknown 1           concentration of unknown 2             Calculate the concentration of the unknowns and answer the following question: Did you need to do any manipulations before applying the…

suctose density gradient ultractifugation is a powerful technique for fractionating macromolecules like DNA,RNA and proteins.some protocols using sucrose gradients mention the following:10 mL sucrose gradients 10-15%(w/v) in 10 mM HEPES buffer.How would you prepare this sucros gradient?

A protein required 6.8 min to travel 82 cm to the detector in a 96 cm -long capillary tube with 25.4 kV between the ends. Find the apparent electrophoretic mobility. How many femtomoles of 2.4 μM protein are injected electrokinetically into a 50 μm diameter capillary at 5.0 kV for 3.0 sec. if the sample has half of the conductivity of the background electrolyte.

Using a detailed scheme, propose a step-wise protocol to purify protein B by ion exchange chromatography (Explain your logic/choices).

Can you please help me to complete step by step the Log molecular weight I will appreciate your help

How could you improve upon your technique in order to get a better and more accurate standard curve graph? 2-Estimate (from your data) the [Protein] of your unknown based on comparing to the standards. Include the correct unit. This estimate should be an integer (no decimals).

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Consider a crude extract with a mixture of the 5 proteins listed below. Protein A 4.5 pl 160 molecular weight, kDa Protein B 12.5 pl and 65 molecular weight Protein C 5.0 pl, 15 molecular weight Protein D 6.8 pl, 150 molecular weight Protein E 9.5 pl, 45 molecular weight You load this protein mixture onto an anion exchange column at pH 11. Next, you apply a "washing" step by passing through buffer at pH 11. Finally, for your elution step, you apply a pH gradient starting from pH 11 to pH 2.0 (A gradient buffer system allows you to gradually and continuously change the pH of your mobile phase starting from pH 11 up to pH 2). You load this same protein mixture onto a Size Exclusion column. Please indicate the order in which these proteins will elute for both. Group of answer choices Yes or No, please explain your answer. If your protein of interest is protein A, would using anion exchange column be completely successful at separating it from all the other proteins? Group of answer…

Fill the table given the info below. Please thank you. Protein at 1 mg/mL which is also 1g/L. Use the DNA sequence below to export to ExPASy Translate & ProtParam. (I tried doing so and I calculated a Molarity of 16.51uM which came from the 60,567.28Da from ExPASy). Using the molarity then use it to fill out the table.…

The calibration curve shown below was used to analyze an unknown protein solution. What is the concentration of the unknown solution, if the absorbance of the unknown is 0.505? Answer in ug/mL. 1.2 y%3D0.005x+0.061 R=0.992 0.8 0.6 0.4 0.2 50 100 150 200 250 Concentration ug/ml Absorbance

Hand draw the expected gel result from the graphical data of three extracted RNA samples (in Figure 1a, 1b, & 1c) in Nanodrop spectrophotometer. The 3 graphical data should be in 1 agarose gel Provide complete gel label descriptions (ladder, lanes, etc.).

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

topic: Bradford AssayThere are numerous methods of protein determination in use, but this module focuses on the Bradford assay.The Bradford assay is a dye-binding method that employs Coomassie Brilliant Blue G-250, whose structureis shown in Figure 2.3.4.1. Coomassie Brilliant Blue G-250 is a dye that interacts with proteins throughhydrophobic and electrostatic interactions.     What are the identities and functions of the components of the Bradford reagent in protein contentdetermination?