QUESTION 1Which protein standard curve would you use to read off the protein concentration of an unknown sample with an absorbancy value of 1.1051.751.501.251.000.750.50-O- BSA+ BGG0.25 -0.005001,0001,5002,000Protein Concentration (pg/ml)Download image.O BSA standard curveO BGG standard curveO Either BSA or BGG standard curvesO Neither BSA or BGG standard curvesNet Absorbance (595 nm)

Proteins are composed of twenty standard amino acids attached together via peptide bonds. Protein's…

Answered: Which protein standard curve would you…

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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The non linear part of the Standard curve graph can be used for estimating the unknown sample protein concentration? True False
#2
A flat (not spherical) tissue engineered skin (thickness 2.5 mm) is attached to the bottom of a dish and cultured with cell media atop it (which has an oxygen concentration of 0.15 mol/m3). The diffusivity of oxygen in the skin is 3.4 E-9 m2/s, and according to experiments that you’ve performed, you want to make sure that the concentration of oxygen in the device doesn’t fall below 0.06 mol/m3. (Below that concentration harms the cells.) The rate of oxygen consumption is -5.9 E-17 mol/[cell◦s]. What is the maximum cellularity (in cells/mL, three significant digits) that this tissue engineered skin can support?
Please help even if its just an explanation on how to do this. I am so confused. Thank you so much
Standard curves You are setting up a standard curve for lysozyme. You have a stock vial containing 2 mg/ml of lysozyme and you have 2 ml in the vial. You will want to have a minimum of 1 ml of each concentration for the spectrophotometer. How would you proceed? (Saline is added to make the various concentrations). Concentration Am't stock lysozyme or am't of a previous dilution (note which) Amount saline Total volume wanted 1.00 mg/ml 0.75 mg/ml 0.50 mg/ml 0.375 mg/ml
What is the minimum length of the column required to completely separate the amino acids? What is the time required for solvent elution (i.e. time for all amino acids to exit the column)?
Which of the following options shows the correct order of fastest to slowest motion of chloride ions, glycine and proteins through the separating gel? Chloride ions > Proteins > Glycine Glycine > Chloride ions > Proteins Chloride ions > Glycine > Protein Protein > Chloride ions > Glycine You are trying to separate a mixture of AMP, ADP, and ATP using ion exchange chromatography. Select appropriate supplies for your experiment. A positively charged column, deprotonated buffer, NaCl of same concentration. A positively charged column, protonated buffer, NaCl of increasing concentration. A negatively charged column, protonated buffer, NaCl of increasing concentration You cannot separate nucleotides using ion exchange chromatography.
100ml of LB media with 25 μg/ml of Amp and 100 μg/ml of Kan final concentration. You have 100ml of LB provided and Amp and Kan stocks at 100 mg/ml and 50 mg/ml provided. Determine how much of each antibiotic stock solution you need to add to 100ml of LB to reach desired antibiotic concentration.
You have a 50X stock solution of TAE buffer, but you need 2 L of a 1X solution for electrophoresis. How much stock should you use?
13. Linear regression analysis was performed for the calibration standard data set based on this experiment. The analysis yielded the following results: m = 59.8805, b = -0.0042. What is the concentration of protein (mg/mL) in the original unknown protein solution if the measured absorbance is 0.736? The absorbance of a blank solution is 0.232. Assume a dilution factor of 40 for the analyzed unknown solution. 0.334 0.3225 0.339 0.3395
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.

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