1.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 in both the folded and unfolded form Its AGO for unfolding is 1.2 kcal/mol at 37° (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 10-fold dilution of your pure protein in solution (by this, we mean that 100 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? B) What is the concentration of the unfolded form of the protein in your sample?

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 in both the folded and unfolded form            Its ΔGo for unfolding is 1.5 kcal/mol at 37o  (where RT = 0.59 kcal/mole) A) 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? B) What is the concentration of the unfolded form of the protein in your sample?

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?

A series of standard proteins and an unknown enzyme were studied by gel filtration on a Sephadex G200 (the 200 refers to the maximum pore size in kDa) column. The elution volume Vel for each protein is given in Table 1 below. (a) Plot the data in the form of log Mr versus elution volume.  From the line of best fit through the points for the standards, determine the Mr of the unknown enzyme.  Explain why ferritin and ovomucoid behave anomalously.                                                      Table 1 - The Vel versus Mr data    Protein               Mr Vel (mL) Blue dextran* Lysozyme Chymotrypsin Ovalbumin Serum albumin Aldolase Urease Ferritin# Ovomucoid# Unknown 1,000,000 14,000 25,000 45,000 68,500 150,000 500,000 700,000 28,000 ⎯ 85 200 190 170 150 125 90 92 160 139                 *Blue dextran is not a protein but a high-Mr carbohydrate that has a covalently bound blue dye, and it elutes with the void volume of the column.                     # Do not…