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 [Protein (BSA)) (pg/ml) 10

A gel filtration column with a fractionation range of 1.5-20 kDa is used to separate out the proteins shown below. If these proteins are collected into separate fractions in between the void volume and total volume, in which order will they elute? Indicate if any of the proteins are found in the void volume or total volume fractions.                                                                        Protein Z - 3330Da                                                                        Protein Y - 13kDa                                                                        Protein X - 1.3kDa I. Total volume fraction II. Third protein fraction III. Second protein fraction IV. First protein fraction V. Void volume fraction

Does this calculation look correct? My goal isto have a target mass of 10 µg of my protein with a total volume of 30 µl. Protein was measured and found to have a concentration of at 308.35 µg/ml Recall, mass = concentration * volume 10 µg = 308.35 µg/ml * V V = 0.01 mg/ 0.30835 mg/mL = 0.032430679 mL = 32.43067942 µL Note: cannot measure this amount; two dilutions required. Dilute by 1/40: measure 2.5 µl of protein at 0.30835 µg/µl and add it to 97.5 diluent to prepare a solution of protein at 7.71 mg/ml. This diluted sample will be used further. Mass = concentration * volume 10 µg = 7.71 mg/ml * V V = 0.01 mg/ 7.71 mg/ml = 1.3 µL Therefore, will measure 1.3 µl of protein at 7.71 mg/ml and add it to 28.7 µl of diluent.

You are studying a protein-protein interaction in 2 proteins. You decide to test both these proteins in different buffers and see if the interaction is preserved. You run the assay in the following buffers, pH 7.4, pH 7.4 with BME, pH 4.5, pH 3.5, pH 11, pH 12.5. The SDS gels from the assays are attached.  a. What type of protein-protein interaction do these results suggest? b. What amino acids are most likely involved in this interaction?

A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).

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?

What is the chemistry behind of the effect of proteins when it is subjected to different temperatures done in three trials? see the data below to interpret Table 3.1 %Transmittance of Identical 10% albumin samples subjected to different temperatures done in three trials. Heating Tempt. (C)   %Transmittance Trial 1 Trial 2 trial 3 Average Control (unheated) 62 62 62 62 55 60 59 58 59 60 2.5 4.5 4.5 11.5 65 1.52 1.6 1.52 1.55 70 1 1 1 1   Table 3.2 Absorbance of Identical 10% albumin solution subjected to different temperatures done in three trials. Heating Tempt. (C)                   Absorbance Readings (450nm) Trial 1 Trial 2 Trial 3 Average Control (unheated) 0.2076 0.2076 0.2076 0.2076 55 0.2218 0.2219 0.2366 0.2292 60 1.6021 1.3468 1.3468 0.9393 65 1.8182 1.7959 1.8182 1.897 70 2 2 2 2

Make a table with a scale of absorbance and the concentration of protein in Chromatin sample from the following data for excel graph Absorbance=660nm following data are of tubes with concern  A =0 B=0.036 C=0.011 D=0.001 E=0.027 F=0.020 G=0.032 H1=0.176 H2=0.183 I1=0.150 I2=0.171 also plot the graph??

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

A sample mixture consists of three proteins with the following properties: Protein A MW (kDa) 200 Amino acid composition 40% nonpolar, 60% polar B 45 20% nonpolar, 80% polar C 98 85% nonpolar, 15% polar IpH 9 3 5 1. If the mixture is subjected to ammonium sulfate precipitation, which protein will precipitate out first? [Select] 2. If the mixture is subjected to isoelectric focusing, which protein will stop moving nearest to the positive electrode? [Select] 3. If the mixture is subjected to cation-exchange chromatography using a buffer at pH 7, which protein will bind to the resin? [Select] 4. If the mixture is subjected to SDS-PAGE, which protein will be at the bottommost portion of the gel? [Select] * Previous Nex