Using the data from the standard curve done previously, you record the absorbance of your extracted milk protein sample at 0.499 at 540nm. What is the mass of the protein in mg assuming you collected 10mL worth of the protein? Your standard curve should have a line of best fit with the equation y=0.0001x+0.0038.

You assay 0.5 ml of 1/2000 diluted egg white for protein, as described in the practical schedule, and the spectrophotometer reading at 595 nm is 0.6. Using the attached calibration curve(click to enlarge), calculate the concentration of protein in undiluted egg white. Give your answer 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).

A series of bovine serum albumin (BSA) was prepared and 1 mL of each solution was subjected to a Bradford assay. The increase in absorbance at 595 nm relative to the concentration of protein was plotted as shown below. Save 1.0- 0.8- 0.6- 0.4- 0.2- 0.04 0.0 0.5 1.0 2.0 2.5 1.5 BSA concentration (mg/mL) a) Using the graph, calculate the original concentration of protein present in a mixture of haemoglobin and methylene blue (diluted 1:50), which gave an absorbance of 0.20 at a wavelength of 595 nm using the Bradford assay. Show all workings. Absorbance (O.D.)

Mn (s) + 2 CuCl (aq) --> 2 Cu (s) + MnCl2 How many grams of Cu will be produced by 2.9 moles of Mn? Round your answer to 2 decimal places.

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?

The standard curve provided below will allow you to answer the remaining questions. Generic Standard Curve 0.7 y = 0.9425x- 0.0034 0.6 0.5 0.4 0.3 02 0.1 0.1 0.2 0.3 0.4 0.5 0.6 0.7 Concentration (mg/ml) - Please describe two ways in which you could use this standard curve to determine the concentration of a pigment in an unknown sample.| #1: #2: -What is your rough estimation of the concentration if you determine the absorbance of a sample is 0.150? Absorbance

When 300 mL of 0.0010 M Ca( NO3)2 solution is added exactly to 500 mL of 0.0015 M K3PO4 solution, find the ion product Q and decide whether to precipitate. (However, K_sp of Ca3(PO4)2 = 1.2x 10^-26)

Consider the fluorescence spectra for bovine serum albumin (BSA) below. One solution contains phosphate buffered saline (PBS), while the other contains 1M HCL. Why does the fluorescence change the way it does? I.e., why do we observe a higher peak and a shift to the left under the presence of acid?

A mixture of five proteins are analyzed by MALDI-TOF. Their molecular weigths are 3 kD, 22 kD, 100 kD, 225 kD and 515 kD. A peak appears in the mass spectrum at 33.3 kD. Which protein most likely gave this peak?