why is it neccessary to have zero a 0 sample (no protein) as part of a standard curve?
Answer: The necessity to have zero a sample or setting blank (no protein ) as a part of standard curve is to zero the background absorbance caused by the reagent. After setting blank or zero the (no protein) sample will give the correct concentration of protein present in the different concentrations of the reagent or solution.
why is it neccessary to have zero a 0 sample (no protein) as part of a...
0. 0 0026 0.987 What is the protein concentration in an unknown food sample with the absorbance value of 0.37 Use the standard curve above 2.83 ug 2.838 0.0002 yg 2.83 mg
You have obtained 150 µL of a protein sample of which you want to perform a Bradford Assay. You perform a 10-fold dilution of your sample and use 10 µl of this dilution to quantify the amount of protein using a Bradford assay. You obtain an absorbance value of 0.63. Using the standard curve and equation you obtained in class, determine the concentration of protein (µg/µL) of your original sample. Show your work. equation: y=0.0139x-0.0153
In biochemistry, we use a 'Bradford Assay' to calculate the concentration of protein in a sample. This method uses the same principles of the standard curve from this experiment. In a Bradford Assay, a standard curve is prepared using a known protein, typically Bovine Serum Albumin (BSA), but rather than measuring the density, we can measure a different property - its 'absorbance'. The graph below is representative of a standard curve from a Bradford Assay (with the line equation displayed...
1. why might a protein have multiple domains. 2.why a protein might be comprised of more than one chain. 3.why a protein structure might show gaps when the real protein has none. 4.why a protein might bind nucleic acids. 5.why a protein might have disulfide bonds. 6. are ligands important for function or just artifacts of the structure process? 7. Why would the surface of a membrane-bound protein have a different polarity from a soluble one?
Sample 1: Protein A in a sample buffer with B-Mercaptoethanol. Sample 2 Protein A in a sample buffer without B-Mercaptoethanol. Sample 3: Protein B in a sample buffer with B-Mercaptoethanol. Sample 4: Protein C in a sample buffer without B-Mercaptoethanol. A. Fill the table below, based on the characteristics of the proteins and the components of the sample buffer. (12 points) Sample 1 Sample 2 Sample 3 Sample 4 Molecular weight 55 kn | 55k Da 52 +57 KDA 5257...
You determine that the protein content of flour sample is 10.25% with a standard deviation of 0.13%. If you will only accept flour sample that have protein content within 2 standard deviations of the mean, what range of protein content will you accept?
SDS Page Gel: The provided standard protein sample for electrophoresis consists of 9 polypeptides with molecular weights ranging from 250 to 15 KDa. Sample 1: Protein A in a sample buffer with B-Mercaptoethanol Sample 2: Protein A in a sample buffer without B-Mercaptoethanol Sample 3: Protein B in a sample buffer with B-Mercaptoethanol Sample 4: Protein C in a sample buffer without B-Mercaptoethanol Use the picture below & the information about the proteins above to answer the following questions. 1a....
You have purified a sample of your protein of interest and have measured the A280 of a 1 in 3 dilution of the protein sample (1 cm pathlength). The value you have obtained for A280 was 0.576. Given that you do not know the sequence of your protein, calculate the approximate concentration of your original protein sample in mg/mL. Give your answer to 2 s.f.
6. If you have two proteins with unknown concentrations (4 points): -sample A: a protein that contains polar uncharged amino acids, negatively charged amino acids and arginines, size: 40 KDa -sample B: a protein rich in lysines, size: 100 KDa A. If you want to separate both proteins, which acrylamide gel concentration would you chose? B. Which staining method (s) would you chose for this gel? Why?
please answer 1 and 2 table 4 protein concentrations 1. Determine the protein concentrations for your positive and negative control and your test sample (Table 4) using the protein standard curve you constructed. Include Table 4 and your protein concentrations in your response. Do these results seem accurate to you? Did they differ from what you expected for the food item you brought into class? 2. What is the R2 value of your known protein concentrations plotted against their absorbency?...