13. Linear regression analysis was performed for the calibration standard data set based on this experiment. The analysisyielded the following results: m = 59.8805, b = -0.0042. What is the concentration of protein (mg/mL) in the originalunknown protein solution if the measured absorbance is 0.736? The absorbance of a blank solution is 0.232. Assume adilution factor of 40 for the analyzed unknown solution.0.3340.32250.3390.3395

Concentration of any unknown sample can be found out from a standard curve. The standard curve is…

Answered: 13. Linear regression analysis was…

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 for the last question "I am not sure how to answer 6a-d" Also if you could answer 4 and 5 as well
Please answer the question below and show all your work. You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole^-1 cm^-1 Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20- fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution?
This is a question regarding spectrophotometry. Scenario: 0.1 mL of the unknown and 0.9 mL of distilled water are mixed in a cuvette and the absorbance is measured at 280 nm. Given the absorbance, molecular mass and the extinction coefficient of the unknown are 0.253, 16950 g and 13940 M-1cm-1 respectively, and the path length is 1 cm, how can I find the concentration of the unknown in mg/mL by Beer-Lambert Law (NOT molarity M)?
You are to prepare capsules that contain 0.125 g of a drug. You have four partial containers of medicatiog, which weigh 3.2 g, 1.784 g, 2.46 g, and 5.87 g. Assume you have weighed each of the four containers with the same scale, and the accuracy is known to the hundredth gram. a Which amount will need to be rounded? b. Which amount is not as accurate as it should be? c. What is the amount of the medication that will be left over after making as many 0.125 g capsules as possible?
can someone explain these calculations to me?
(please type answer with explanation).
Given a stock protein solution with a concentration of 6 mg/ml, determine the protein concentration of a solution made by mixing 5 μl of the stock with 5 μl of a buffer.
The following data is protein melting point (Tm) characterization data obtained by the Zetasizer Nano System (Dynamic Light Scattering method, DLS)². The melting point for the series of proteins are measured in PBS (phosphate buffered saline). Which protein is structurally the most stable form in PBS? State your reasoning in full sentence. Z average in DLS: The dynamic size of particle. * 100 Protein T.(°C) 38 65 71 64 68 90 Bovine Hemoglobin Bovine Serum Albumin Ovalbumin Human Insulin Hen Egg Lysozyme 80 70 60 50 40 30 20 10 30 35 40 45 50 55 60 65 70 75 80 Temperature (°C) Z Average Diameter (nm)
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.
A calibration curve for the absorbance of an unknown is shown below. What would be the concentration of a sample with absorbance of 0.45. Give the answer with the correct unit.
Various concentrations of recombinant human insulin were prepared for use standards for an HPLC method. To verify the prepared concentrations, the samples were analyzed by measuring the absorbance at 280 nm in a short path length (5 mm) cuvette. The molar absorption coefficient for human insulin is approximately 5.875 x 10³ M-¹cm-¹. a. Calculate the extinction coefficient in mL mg-¹cm-¹. b. Calculate the concentrations of the following human insulin standards if the measured absorbances and dilutions used are: Standard 1 Standard 2 Abs. (at 280 nm) of Diluted Sample 0.305 0.685 Dilution 145.0 µL sample, 25.0 μL buffer 130.0 µL sample, 40.0 μL buffer
You assay 0.5 ml of 1/2000 diluted egg white for protein, as described in the practical schedule, and the spectrophotometer reading at 595 nm is 0.6. Using the attached calibration curve(click to enlarge), calculate the concentration of protein in undiluted egg white. Give your answer in mg/ml.

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