Using ultrafiltration, you concentrate a solution of Protein X as follows: Initial volume protein X = 300 mL Initial concentration protein X = 12 mg/mL Final volume protein X = 15 mL What's the final concentration of protein X in mg/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).

Why are integral proteins more difficult to study then peripheral, and why integral can only be isolated with strong deteargents.

Give typed full explanation

Is an SDS-PAGE gel, what characteristic is used to separate the proteins?  Which proteins move quickly? Which ones move slowly?

In addition to our purified DHFR sample, we will also be including three other protein samples as controls. Of the different protein samples analyzed, which protein will travel the slowest/least distance through the SDS-PAGE gel? A) The smallest protein analyzed B) The largest protein analyzed C) Although different in size, all proteins analyzed will travel the same distance on the gel

d/e/1FAIpQLSfTle9UfP15_VUqFI-ACEQd1XBykXv5Lr4dEMQbLJ1d6fCupw/viewform Students subjected three samples of five different molecules to gel electrophoresis as shown in Figure 1 A B C DE +2 3 Wells 4 8. Which of the following statements best explains the pattern seen on the * gel with regard to the size and charge of molecules A and B? 1 point molecules A and B are positively charged, and molecule A is smaller than molecule B. molecules A and B are positively charged, and molecule A is larger than molecule B. molecules A and B are negatively charged, and molecule A is smaller than molecule B. molecules A and B are negatively charged, and molecule A is larger than molecule B. Sign out

Match each stated goal to the most relevant method, technique, or procedure for achieving that goal. -isoelectric focusing -salting out - differential centrifugation - Edman degradation - ion exchange -dialysis - gel filtration A) removing K+ ions from a protein sample B) Removing large cellular debris from the initial cell lysate C) Isolating small proteins from a solution that also contains large proteins D) separating two proteins that differ greatly in their ionic solubility E) separating two proteins that differ by the magnitude of charge on their surface

To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?

To analyze a sample by mass spectrometry, the sample must consist of gas phase ions. a) Explain why it is difficult to make gas phase ions of proteins.   b) Generally explain how electrospray ionization turns proteins in solution into gas phase ions.